ID   AHBB_OLEA2              Reviewed;         158 AA.
AC   Q30WH3;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Siroheme decarboxylase beta subunit {ECO:0000305};
DE            EC=4.1.1.111 {ECO:0000269|PubMed:21969545};
GN   Name=ahbB {ECO:0000303|PubMed:21969545};
GN   OrderedLocusNames=Dde_3179 {ECO:0000312|EMBL:ABB39973.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21969545; DOI=10.1073/pnas.1108228108;
RA   Bali S., Lawrence A.D., Lobo S.A., Saraiva L.M., Golding B.T., Palmer D.J.,
RA   Howard M.J., Ferguson S.J., Warren M.J.;
RT   "Molecular hijacking of siroheme for the synthesis of heme and d1 heme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18260-18265(2011).
CC   -!- FUNCTION: Involved in siroheme-dependent heme b biosynthesis. Catalyzes
CC       the decarboxylation of siroheme into didecarboxysiroheme.
CC       {ECO:0000269|PubMed:21969545}.
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:21969545};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000269|PubMed:21969545}.
CC   -!- SUBUNIT: Forms an heterodimer composed of AhbA and AhbB.
CC       {ECO:0000269|PubMed:21969545}.
CC   -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR   EMBL; CP000112; ABB39973.1; -; Genomic_DNA.
DR   RefSeq; WP_011368927.1; NC_007519.1.
DR   AlphaFoldDB; Q30WH3; -.
DR   SMR; Q30WH3; -.
DR   STRING; 207559.Dde_3179; -.
DR   DNASU; 3758154; -.
DR   EnsemblBacteria; ABB39973; ABB39973; Dde_3179.
DR   KEGG; dde:Dde_3179; -.
DR   eggNOG; COG1522; Bacteria.
DR   HOGENOM; CLU_112007_0_1_7; -.
DR   OMA; NLFCMVH; -.
DR   OrthoDB; 1844486at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002710; Chromosome.
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; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF17805; AsnC_trans_reg2; 1.
DR   SMART; SM00344; HTH_ASNC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Heme biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..158
FT                   /note="Siroheme decarboxylase beta subunit"
FT                   /id="PRO_0000450506"
SQ   SEQUENCE   158 AA;  18223 MW;  08DAF2C22A1F2969 CRC64;
     MAQTFTDTER AILRIVQKNL PDSATPYADI AEQTGTDEQT VLALLRRMKE EGSIRRFGAS
     LKHQKAGYTH NAMVAWIVDK DTVDEVGRQA AEHRLISHVY YRPSTAPDWP YTLYTMIHGR
     HENEYLEVID TLRKETALEE YAVLNSLKEL KKTSMTYF