Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup SPASM/twitch domain containing

  ⌊ main SPASM domain-containing

  ⌊ heme carboxy lyase like

     ⌊ Family alternative heme biosynthesis C (AhbC-like)

  ⌊ FunctionalDomain alternative heme biosynthesis C (AhbC) (ID 411106)

Superfamily Assignment Evidence Code(s) ISS PubMed:24713144
Family Assignment Evidence Code CFM PubMed:24713144
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Desulfovibrio desulfuricans Taxon ID: 876 501717989 WP_012623934.1 (RefSeq)
Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774 Taxon ID: 525146 219867869 ACL48204.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1K1N1V3 A0A1K1N1V3_DESDE (TrEMBL)
n/a B8J367 B8J367_DESDA (TrEMBL)

Sequence

Length of Enzyme (full-length): 394 | Length of Functional Domain: 394

1       10        20        30        40        50        60

MIGISKLYCGQVEPSDALRYGRESGKLPSHLLQFSKDKKPVVVWNMTQRCNLKCVHCYAH
AIEVDGTDDINTQQAKAMIDDLAAYGAPVMLFSGGEPLVRKDLVELASHATSKGMRAVIS
TNGTLITKEKARELKAVGLSYVGISLDGMEEIHDKFRAVPGAFRKALEGIANCQAEGLKV
GLRLTINKRNAGEIPGIFRLLKDMEIPRACFYHLVYSGRGSELIKEDLDHAETRQVLDLI
MDETRALFDAGKGKEILTVDNHADGPYVWMRLKREDPKRAEEVFELLQYNEGNSSGRGIG
CISWDGKVHADQFWRNHVLGNVLERPFSQIWDDPSIELLHKLKDKKAHVKGRCAKCRFLN
ICGGNFRARAEAYYDDIWAQDPACYLTDEEIGLK
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
50 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
54 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
57 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 7/7 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
50 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
54 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
57 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
353 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
356 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
362 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
384 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
50 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:24713144
54 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:24713144
57 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:24713144
353 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS PubMed:24713144
356 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS PubMed:24713144
362 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS PubMed:24713144
384 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS PubMed:24713144

Catalyzed Reaction

didecarboxysirohaem deacetylase

+ 2 + 2 + 2 + 2
12,18-didecarboxysiroheme
132253		 S-adenosyl-L-methionine zwitterion
59789		 Fe-coproporphyrin III
60454		 acetic acid
15366		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 2:59 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 270 394
update domain start position 32 2
June 14, 2014, 2:53 a.m. update domain start position 2 1
Oct. 15, 2016, 6:07 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update subgroup SPASM/twitch domain containing heme carboxy lyase like
EC number assigned by UniProtKB accession ID.