AHBA_DESDA
ID AHBA_DESDA Reviewed; 173 AA.
AC B8J364;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Siroheme decarboxylase alpha subunit {ECO:0000305};
DE EC=4.1.1.111 {ECO:0000269|PubMed:24865947};
GN OrderedLocusNames=Ddes_0286 {ECO:0000312|EMBL:ACL48201.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4CZD, ECO:0007744|PDB:4UN1}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEXES WITH AHBB AND
RP DIDECARBOXYSIROHEME, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=24865947; DOI=10.1111/mmi.12656;
RA Palmer D.J., Schroeder S., Lawrence A.D., Deery E., Lobo S.A.,
RA Saraiva L.M., McLean K.J., Munro A.W., Ferguson S.J., Pickersgill R.W.,
RA Brown D.G., Warren M.J.;
RT "The structure, function and properties of sirohaem decarboxylase--an
RT enzyme with structural homology to a transcription factor family that is
RT part of the alternative haem biosynthesis pathway.";
RL Mol. Microbiol. 93:247-261(2014).
CC -!- FUNCTION: Involved in siroheme-dependent heme b biosynthesis. Catalyzes
CC the decarboxylation of siroheme into didecarboxysiroheme
CC (PubMed:24865947). Siroheme is decarboxylated to monodecarboxysiroheme,
CC which is in turn decarboxylated to didecarboxysiroheme
CC (PubMed:24865947). {ECO:0000269|PubMed:24865947}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2;
CC Xref=Rhea:RHEA:19093, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:60052, ChEBI:CHEBI:140497; EC=4.1.1.111;
CC Evidence={ECO:0000269|PubMed:24865947};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.74 uM for siroheme {ECO:0000269|PubMed:24865947};
CC KM=9.94 uM for monodecarboxysiroheme {ECO:0000269|PubMed:24865947};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:24865947}.
CC -!- SUBUNIT: Forms an heterodimer composed of AhbA and AhbB.
CC {ECO:0000269|PubMed:24865947}.
CC -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR EMBL; CP001358; ACL48201.1; -; Genomic_DNA.
DR PDB; 4CZD; X-ray; 2.23 A; A/C=1-173.
DR PDB; 4UN1; X-ray; 1.97 A; A/C=1-173.
DR PDBsum; 4CZD; -.
DR PDBsum; 4UN1; -.
DR AlphaFoldDB; B8J364; -.
DR SMR; B8J364; -.
DR STRING; 525146.Ddes_0286; -.
DR EnsemblBacteria; ACL48201; ACL48201; Ddes_0286.
DR KEGG; dds:Ddes_0286; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_112007_1_0_7; -.
DR OMA; NVWFTFI; -.
DR BRENDA; 4.1.1.111; 1905.
DR UniPathway; UPA00252; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR040523; AsnC_trans_reg2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF17805; AsnC_trans_reg2; 1.
DR Pfam; PF13404; HTH_AsnC-type; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme biosynthesis; Lyase.
FT CHAIN 1..173
FT /note="Siroheme decarboxylase alpha subunit"
FT /id="PRO_0000450503"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24865947"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24865947"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:4UN1"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 134..148
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4CZD"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:4UN1"
SQ SEQUENCE 173 AA; 19191 MW; 62B8F929472DCA7D CRC64;
MTTQTSAATG SPTQQNNAAL ADMDSMDRQL LDIIQTGFPL SPRPYAELGQ RLGLDEQEVL
DRVRGLKARK IIRRLGANFQ SAKLGFVSTL CAAKVPQDKM DAFVAEVNAK PGVTHNYLRE
HDYNIWFTLI SPSREETQAI LDGITQATGV PILNLPATKL FKIRVDFRMD NDS
