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Database: UniProt
Entry: I0I3W2_CALAS
LinkDB: I0I3W2_CALAS
Original site: I0I3W2_CALAS 
ID   I0I3W2_CALAS            Unreviewed;       311 AA.
AC   I0I3W2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   ECO:0000313|EMBL:BAL99949.1};
GN   OrderedLocusNames=CLDAP_19100 {ECO:0000313|EMBL:BAL99949.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99949.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL99949.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000256|HAMAP-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; AP012337; BAL99949.1; -; Genomic_DNA.
DR   RefSeq; WP_014433185.1; NC_017079.1.
DR   AlphaFoldDB; I0I3W2; -.
DR   STRING; 926550.CLDAP_19100; -.
DR   KEGG; cap:CLDAP_19100; -.
DR   PATRIC; fig|926550.5.peg.2120; -.
DR   eggNOG; COG0181; Bacteria.
DR   HOGENOM; CLU_019704_0_2_0; -.
DR   OrthoDB; 9810298at2; -.
DR   UniPathway; UPA00251; UER00319.
DR   Proteomes; UP000007880; Chromosome.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; PF01379; Porphobil_deam; 1.
DR   Pfam; PF03900; Porphobil_deamC; 1.
DR   PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
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:UP000007880};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          8..213
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          230..298
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   MOD_RES         245
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   311 AA;  32870 MW;  1B20BF15B73439A9 CRC64;
     MSERIDAVRL GTRGSMLARW QTDYVAGLLA KAWPHLHIHV EVLHTQGDRV LDRPLPVIGG
     KGLFTAELEE ALHSGAIDLA VHSLKDLPIE LASGLTIGAI PTRGAVHDVV ISRSGHPLAQ
     LPAGATVGTS SRRRSAQLLR ACPHLRTIDI RGNVDTRIRK TLDPAGPYDA IVLAAAGIER
     LGRPDAVTEA LSLEIMLPAP GQGALAVQCR DDAAILRLLV PLEDPVTRVA VTAERAFLRH
     VGGGCAVPVA AYAQITAGRL HLRGRVLSPD GRRCIEVEGD SHPDEPEMLG AKLAAQALAQ
     GAASLLAEET S
//
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