ID A0A060JB85_9MICO Unreviewed; 558 AA.
AC A0A060JB85;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Porphobilinogen deaminase {ECO:0000256|HAMAP-Rule:MF_00260};
DE Short=PBG {ECO:0000256|HAMAP-Rule:MF_00260};
DE EC=2.5.1.61 {ECO:0000256|HAMAP-Rule:MF_00260};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|HAMAP-Rule:MF_00260};
DE Short=HMBS {ECO:0000256|HAMAP-Rule:MF_00260};
DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|HAMAP-Rule:MF_00260};
GN Name=hemC {ECO:0000256|HAMAP-Rule:MF_00260};
GN ORFNames=Rhola_00002880 {ECO:0000313|EMBL:AIC47111.1};
OS Rhodoluna lacicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Rhodoluna.
OX NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC47111.1, ECO:0000313|Proteomes:UP000067708};
RN [1] {ECO:0000313|EMBL:AIC47111.1, ECO:0000313|Proteomes:UP000067708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC47111.1,
RC ECO:0000313|Proteomes:UP000067708};
RX PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT with stream-lined genome.";
RL Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the
CC hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
CC {ECO:0000256|ARBA:ARBA00002869, ECO:0000256|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:0000256|ARBA:ARBA00000416, ECO:0000256|HAMAP-
CC Rule:MF_00260};
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00260};
CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000256|HAMAP-
CC Rule:MF_00260};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the
CC dipyrromethane group. {ECO:0000256|HAMAP-Rule:MF_00260}.
CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000256|ARBA:ARBA00005638,
CC ECO:0000256|HAMAP-Rule:MF_00260}.
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DR EMBL; CP007490; AIC47111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060JB85; -.
DR STRING; 529884.Rhola_00002880; -.
DR KEGG; rla:Rhola_00002880; -.
DR PATRIC; fig|529884.3.peg.274; -.
DR eggNOG; COG0181; Bacteria.
DR HOGENOM; CLU_036069_0_0_11; -.
DR OrthoDB; 9810298at2; -.
DR Proteomes; UP000067708; Chromosome.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:InterPro.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06578; HemD; 1.
DR Gene3D; 3.40.50.10090; -; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 1.
DR HAMAP; MF_00260; Porphobil_deam; 1.
DR InterPro; IPR036108; 4pyrrol_syn_uPrphyn_synt_sf.
DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
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 NCBIfam; TIGR00212; hemC; 1.
DR PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 1.
DR Pfam; PF02602; HEM4; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF69618; HemD-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE 3: Inferred from homology;
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW Rule:MF_00260}; Reference proteome {ECO:0000313|Proteomes:UP000067708};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00260}.
FT DOMAIN 6..210
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 225..298
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT DOMAIN 327..550
FT /note="Tetrapyrrole biosynthesis uroporphyrinogen III
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02602"
FT MOD_RES 240
FT /note="S-(dipyrrolylmethanemethyl)cysteine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ SEQUENCE 558 AA; 59645 MW; AD9E8C73F88A6191 CRC64;
MPSRTLKLGT RGSLLATTQS GMIADQIQTT TGLASELVFI KTEGDNPSSN LFAPKRPGVF
VSALRDALLA GEVDYIVHSF KDLPSAPMPG ITLAAIPRRE DHRDILISRD NQTLSELATG
AVVGTSSPRR AARIRHLRPD LEIKPIRGNI DTRLKKVQDG DFDATILAAA GLNRIGLGEV
NKWFFTDAEL LPAPAQGALA IECRSGDLDL IAELQKVNHA ETELIVTAER AVLRGISASC
TTAIGAHAEL TDGRLTLTAE LSDNETDWHE RVSLSLDAAS SNKAQSLALG LEIAEQLMQT
ELGQKIGTPR EKSVLLVRAT DNELDEAAFK SAGFKVVCDP YLKISKFNNP AGVDRMLEAL
RSAEPGTWLV ITSINSVRFF AEQIGIDNFK AAISNPNLKF AAIGERSAAE IKSLGVQEVL
LAEDSNAGAL STAILKHMPK QVILPASNIA MKTLQDAVVT SGVELITEVV YTTETVPNVP
LSISALKQGE IDVLVLRSPS AARAVANFIS PKDVLALVLV TGNATLEQTR KLGFPRVAMT
SETTPDSLVA TVTSPNMN
//
