AHBB_DESDA
ID AHBB_DESDA Reviewed; 159 AA.
AC B8J3A4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Siroheme decarboxylase beta subunit {ECO:0000305};
DE EC=4.1.1.111 {ECO:0000269|PubMed:24865947};
GN OrderedLocusNames=Ddes_2018 {ECO:0000312|EMBL:ACL49914.1};
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 AHBA AND
RP DIDECARBOXYSIROHEME, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND MUTAGENESIS OF ARG-102.
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; ACL49914.1; -; Genomic_DNA.
DR RefSeq; WP_012625638.1; NC_011883.1.
DR PDB; 4CZD; X-ray; 2.23 A; B/D=1-159.
DR PDB; 4UN1; X-ray; 1.97 A; B/D=1-159.
DR PDBsum; 4CZD; -.
DR PDBsum; 4UN1; -.
DR AlphaFoldDB; B8J3A4; -.
DR SMR; B8J3A4; -.
DR STRING; 525146.Ddes_2018; -.
DR EnsemblBacteria; ACL49914; ACL49914; Ddes_2018.
DR KEGG; dds:Ddes_2018; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_112007_0_1_7; -.
DR OMA; NLFCMVH; -.
DR OrthoDB; 1844486at2; -.
DR UniPathway; UPA00252; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR040523; AsnC_trans_reg2.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF17805; AsnC_trans_reg2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme biosynthesis; Lyase.
FT CHAIN 1..159
FT /note="Siroheme decarboxylase beta subunit"
FT /id="PRO_0000450507"
FT BINDING 152..157
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24865947"
FT MUTAGEN 102
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24865947"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:4UN1"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:4UN1"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:4UN1"
SQ SEQUENCE 159 AA; 17914 MW; 73ED6C666B29AD61 CRC64;
MSHQFSPEEQ AVLRIVQANL PDSLTPYADL AEQAGMTEAQ VLELLGRLKA SGAIRRFGAS
IKHQKTGWTH NAMVAWKVTP DQVDDCGRKA AEHSHISHVY YRPSSAPDWP YEMYTMIHGR
SEAECLGVVE DVKRTTSLKE HAILRSLKEL KKTSMTYFT
