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Database: UniProt
Entry: A0A024GG92_9STRA
LinkDB: A0A024GG92_9STRA
Original site: A0A024GG92_9STRA 
ID   A0A024GG92_9STRA        Unreviewed;       368 AA.
AC   A0A024GG92;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE            EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
DE   AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00033064};
GN   ORFNames=BN9_066210 {ECO:0000313|EMBL:CCI45724.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI45724.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI45724.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI45724.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004735}.
CC   -!- SIMILARITY: Belongs to the HMBS family.
CC       {ECO:0000256|ARBA:ARBA00005638}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI45724.1}.
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DR   EMBL; CAIX01000105; CCI45724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GG92; -.
DR   STRING; 65357.A0A024GG92; -.
DR   InParanoid; A0A024GG92; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR000860; HemC.
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   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..243
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          255..325
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
SQ   SEQUENCE   368 AA;  40391 MW;  6E56702A6996B99C CRC64;
     MTEDSKSRKI IHVASRKSVL AMAQTNEVIE MLQLHPDVDF VVGQTNTLGD QVQDRHLSDL
     GTSIDSGLFT KSLEESLINK TSDFAVHSLK DMPTTLPPGL VLATICKRAS PEDAVIIHPK
     HKRKVLLHSR DLTCLTRTSQ NISRLEELPE QSIIGTSSLR REALLRQMHP SFRMKTIRGN
     IQTRLSKLDD HSEYDAIVVA ACGFRRGGLG NRIDQILPSK DFGYGVGQGS IGIECRADDT
     ETLKMLRQIE HHESALCCKA ERSLLYHLEG GCQISMGVHT TLHNGILTLT ATVLSRDGTK
     SVEDMITGPC EEAVDLGEKL ARRFLANNDA IILLGKIGKK RPLTYGDIEA PGDAAAAAKK
     MRSQGNVV
//
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