HEM3_DESVH
ID HEM3_DESVH Reviewed; 315 AA.
AC Q72AV0;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Porphobilinogen deaminase {ECO:0000255|HAMAP-Rule:MF_00260};
DE Short=PBG {ECO:0000255|HAMAP-Rule:MF_00260};
DE EC=2.5.1.61 {ECO:0000255|HAMAP-Rule:MF_00260};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000255|HAMAP-Rule:MF_00260};
DE Short=HMBS {ECO:0000255|HAMAP-Rule:MF_00260};
DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000255|HAMAP-Rule:MF_00260};
GN Name=hemC {ECO:0000255|HAMAP-Rule:MF_00260}; OrderedLocusNames=DVU_1890;
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).
CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+);
CC Xref=Rhea:RHEA:13185, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57845, ChEBI:CHEBI:58126; EC=2.5.1.61;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00260};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00260};
CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000255|HAMAP-
CC Rule:MF_00260};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000255|HAMAP-Rule:MF_00260}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000255|HAMAP-
CC Rule:MF_00260}.
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DR EMBL; AE017285; AAS96366.1; -; Genomic_DNA.
DR RefSeq; WP_010939176.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011107.1; NC_002937.3.
DR AlphaFoldDB; Q72AV0; -.
DR SMR; Q72AV0; -.
DR STRING; 882.DVU_1890; -.
DR PaxDb; Q72AV0; -.
DR EnsemblBacteria; AAS96366; AAS96366; DVU_1890.
DR KEGG; dvu:DVU_1890; -.
DR PATRIC; fig|882.5.peg.1733; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_019704_0_2_7; -.
DR OMA; LWQANHI; -.
DR PhylomeDB; Q72AV0; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.160.40; -; 1.
DR HAMAP; MF_00260; Porphobil_deam; 1.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
DR InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR PANTHER; PTHR11557; PTHR11557; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF54782; SSF54782; 1.
DR TIGRFAMs; TIGR00212; hemC; 1.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..315
FT /note="Porphobilinogen deaminase"
FT /id="PRO_0000142933"
FT MOD_RES 241
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ SEQUENCE 315 AA; 34040 MW; 2FAF5A2E16E7B114 CRC64;
MKHLVIATRG SKLALWQAEH IKSLIETEHA GKVDVSLKII KTKGDIILDV PLAKVGGKGL
FVKEIEEALL DGSADLAVHS MKDVPMELPE GLFLGCIPER EEPSDTLLSV RYASLDALPH
GARVGTSSLR RQSQLLALRP DLDIISLRGN VDTRLRKLMD GEFDAIVMAT AGLKRLGLAA
PHHEVLAPPR FLPAVGQGAL GIEFREDRAD LRDMLAFLDH RPTRIRVEAE RGFLAGLEGG
CQVPIAGHAV MTGDDNFRIE GLVADLKGER VIRRTLEGTG ANARNRGLEL ASQVLADGAA
EILDEVYASG AADRQ
