HEM3_NITMS
ID HEM3_NITMS Reviewed; 311 AA.
AC A9A1A1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Probable 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=Nmar_0491;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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 -!- 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; CP000866; ABX12387.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A1A1; -.
DR SMR; A9A1A1; -.
DR STRING; 436308.Nmar_0491; -.
DR EnsemblBacteria; ABX12387; ABX12387; Nmar_0491.
DR KEGG; nmr:Nmar_0491; -.
DR eggNOG; arCOG04299; Archaea.
DR HOGENOM; CLU_019704_1_0_2; -.
DR OMA; LWQANHI; -.
DR PhylomeDB; A9A1A1; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..311
FT /note="Probable porphobilinogen deaminase"
FT /id="PRO_1000114166"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00260"
SQ SEQUENCE 311 AA; 34011 MW; 0C4072B4CEF6BC51 CRC64;
MKYIVGARGS QLSVAQTNLV IAELKKAHPD TEYEIKTITT KGDTDSRPLF TIDQKGIFEK
EIDRAVAQKE VDFAVHSLKD VPSELDDNLV LACIPKRETV NDVFISPDGS TLDSIKPGSV
IGTSSLRRAV QVSRKRPDVT VKPIRGNIET RIKKASGENY DAIVLAKAGI SRLGVDVKYT
ELSTDDFSPS PGQGAIAIVA RADDSKTIEM LKKIEDPDSR LEIEAERALS DFVDSGCRFP
VGAYAKSNGS EMTLTVTAFS VDGKQFLHVS KTGDKNNPKS LGQSAGEELR EKGVNDLALN
WREKVEEWNK T