AHBD_DESVH
ID AHBD_DESVH Reviewed; 367 AA.
AC Q72DS4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=AdoMet-dependent heme synthase {ECO:0000305};
DE EC=1.3.98.6 {ECO:0000269|PubMed:21969545};
GN Name=ahbD {ECO:0000303|PubMed:21969545};
GN OrderedLocusNames=DVU_0855 {ECO:0000312|EMBL:AAS95335.1};
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, AND PATHWAY.
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 conversion of Fe-coproporphyrin III into heme by the oxidative
CC decarboxylation of two propionate side chains.
CC {ECO:0000269|PubMed:21969545}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = 2 5'-
CC deoxyadenosine + 2 CO2 + heme b + 2 L-methionine;
CC Xref=Rhea:RHEA:56520, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:60344,
CC ChEBI:CHEBI:68438; EC=1.3.98.6;
CC Evidence={ECO:0000269|PubMed:21969545};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:21969545}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; AE017285; AAS95335.1; -; Genomic_DNA.
DR RefSeq; YP_010076.1; NC_002937.3.
DR AlphaFoldDB; Q72DS4; -.
DR SMR; Q72DS4; -.
DR IntAct; Q72DS4; 2.
DR STRING; 882.DVU_0855; -.
DR PaxDb; Q72DS4; -.
DR EnsemblBacteria; AAS95335; AAS95335; DVU_0855.
DR KEGG; dvu:DVU_0855; -.
DR PATRIC; fig|882.5.peg.799; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_0_7; -.
DR OMA; GWGRQFF; -.
DR PhylomeDB; Q72DS4; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034391; Cmo-like_SPASM_containing.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR030896; rSAM_AhbD_hemeb.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDF00542; alternative_heme_biosynthesis; 1.
DR SFLD; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR04545; rSAM_ahbD_hemeb; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Heme biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..367
FT /note="AdoMet-dependent heme synthase"
FT /id="PRO_0000450512"
FT DOMAIN 15..238
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ SEQUENCE 367 AA; 40909 MW; A30B27DE0AF2935F CRC64;
MGAHPTAHGP RTLEDGSPTC KLIAWEVTRS CNLACKHCRA EAHMEPYPGE FSTDEAKALI
DTFPDVGNPI IIFTGGDPMM RGDVYELIAY ATDKGLRCVM SPNGTLITPE HAQRMKASGV
QRCSISIDGP DAASHDAFRG VPGAFEQSMR GIGYLRDAGI EFQINTTVTR DNLHSFKDIF
KLCERIGAVA WHIFLLVPTG RAAGLSDQVI SAAEYEEVLN WFYDFRKTTS MHLKATCAPH
YYRIMRQRAK EEGVSVTPDN FGMDAMTRGC LGGTGFCFIS HTGQVQPCGY LELDCGNVRN
TPFPEIWRKS EHFRQFRTQE EYTGKCGPCE YHKVCGGCRA RAYNMSGDHM AEEPLCSYKP
RRMTPCR
