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Database: UniProt
Entry: A0A1H0UY51_9MICO
LinkDB: A0A1H0UY51_9MICO
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ID   A0A1H0UY51_9MICO        Unreviewed;       368 AA.
AC   A0A1H0UY51;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN04489867_3568 {ECO:0000313|EMBL:SDP71202.1};
OS   Pedococcus dokdonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Pedococcus.
OX   NCBI_TaxID=443156 {ECO:0000313|EMBL:SDP71202.1, ECO:0000313|Proteomes:UP000199077};
RN   [1] {ECO:0000313|Proteomes:UP000199077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   -!- 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; LT629711; SDP71202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0UY51; -.
DR   STRING; 443156.SAMN04489867_3568; -.
DR   OrthoDB; 9810298at2; -.
DR   Proteomes; UP000199077; Chromosome i.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00260}.
FT   DOMAIN          11..214
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          229..301
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   REGION          306..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         244
FT                   /note="S-(dipyrrolylmethanemethyl)cysteine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00260"
SQ   SEQUENCE   368 AA;  37195 MW;  2343BB2418FA6E55 CRC64;
     MSAPATAPLA LRLGTRRSAL ATTQSGWVAD RLRAHGHTVE LVEIVTEGDT STASLASIGG
     TGVFAAALRR ALLAGEVDFA VHSLKDLPTA AEPGLVVAAV PVREDPRDVL VSSGGRTLGE
     LGEGAVVGTG SPRRVAQLAA LGLGLSFKDI RGNVDTRIGL VRDGALDGVV LARAGLARLG
     RLDDVAEALD PLQMLPAPGQ GALAVECRTD DHVTQAALAV LDDADTRSCV TAERAVLAAL
     EAGCSAPVGA LAEVVEGEDG LELSLRAFVG AVDGSFDLRR SLVGGVDDAE ALGRRLAAVL
     LDDGGDLLRG PEERPPAPDA PGPAGAGPAG SHDAQPPDPP GATGADPLAA TDRSTDRISD
     HDSTERAL
//
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