AHBB_DESVH
ID AHBB_DESVH Reviewed; 160 AA.
AC Q725I2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Siroheme decarboxylase beta subunit {ECO:0000305};
DE EC=4.1.1.111 {ECO:0000269|PubMed:21969545, ECO:0000269|PubMed:24865947};
GN Name=ahbB {ECO:0000303|PubMed:21969545};
GN OrderedLocusNames=DVU_3167 {ECO:0000312|EMBL:AAS97637.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND HEME-BINDING.
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 {ECO:0000269|PubMed:21969545, 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:21969545, ECO:0000269|PubMed:24865947};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:21969545,
CC ECO:0000269|PubMed:24865947}.
CC -!- SUBUNIT: Forms an heterodimer composed of AhbA and AhbB
CC (PubMed:21969545, PubMed:24865947). Also forms heterotetramers
CC (PubMed:24865947). {ECO:0000269|PubMed:21969545,
CC ECO:0000269|PubMed:24865947}.
CC -!- MISCELLANEOUS: Binds heme b, but reducing agents do not affect the
CC activity of the enzyme. {ECO:0000269|PubMed:24865947}.
CC -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR EMBL; AE017285; AAS97637.1; -; Genomic_DNA.
DR RefSeq; WP_010940425.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_012377.1; NC_002937.3.
DR AlphaFoldDB; Q725I2; -.
DR SMR; Q725I2; -.
DR IntAct; Q725I2; 4.
DR STRING; 882.DVU_3167; -.
DR PaxDb; Q725I2; -.
DR DNASU; 2795872; -.
DR EnsemblBacteria; AAS97637; AAS97637; DVU_3167.
DR KEGG; dvu:DVU_3167; -.
DR PATRIC; fig|882.5.peg.2872; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_112007_0_1_7; -.
DR OMA; YNLFAML; -.
DR PhylomeDB; Q725I2; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002194; 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..160
FT /note="Siroheme decarboxylase beta subunit"
FT /id="PRO_0000450508"
SQ SEQUENCE 160 AA; 18419 MW; 44B03E7417D84559 CRC64;
MSRYDDFTEV ERAILRIVQS NLPDSLTPYA DIAREVGTDE ETVLALLRSL KEEGPIRRFG
ASIKHQRAGW NHNAMVAWKV DPAIVEEAGT KAAEHPHISH VYYRPSSAPD WPYELYTMIH
GRHATAHMDV IEQLRRETPL EEFAVLESLR ELKKTSMTYF
