AHBA_DESVH
ID AHBA_DESVH Reviewed; 176 AA.
AC Q72DS5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Siroheme decarboxylase alpha subunit {ECO:0000305};
DE EC=4.1.1.111 {ECO:0000269|PubMed:21969545, ECO:0000269|PubMed:24865947};
GN Name=ahbA {ECO:0000303|PubMed:21969545};
GN OrderedLocusNames=DVU_0854 {ECO:0000312|EMBL:AAS95334.1};
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; AAS95334.1; -; Genomic_DNA.
DR RefSeq; WP_010938154.1; NC_002937.3.
DR RefSeq; YP_010075.1; NC_002937.3.
DR AlphaFoldDB; Q72DS5; -.
DR SMR; Q72DS5; -.
DR IntAct; Q72DS5; 3.
DR STRING; 882.DVU_0854; -.
DR PaxDb; Q72DS5; -.
DR DNASU; 2794183; -.
DR EnsemblBacteria; AAS95334; AAS95334; DVU_0854.
DR KEGG; dvu:DVU_0854; -.
DR PATRIC; fig|882.5.peg.798; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_112007_1_0_7; -.
DR OMA; EVSHNYL; -.
DR PhylomeDB; Q72DS5; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002194; Chromosome.
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 Heme biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..176
FT /note="Siroheme decarboxylase alpha subunit"
FT /id="PRO_0000450504"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 19822 MW; BAB67DE36BCA4EC2 CRC64;
MTEAHNACCH PSGTAAGHHG AGKASTDMMD AVDRRLLDII QTGFPIEPRP YAVLGETLGI
TECEALARVR ALRERKVIRR LGANFDSWKL GFRSTLCAAK VPEDRIDAFV AEVNRHVNVT
HNYLRNHEYN IWFTCICPSW EQVCSLLDGI TERTGIPILN LPATKLYKIR VDFRMD
