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Database: UniProt
Entry: O50320_PORGN
LinkDB: O50320_PORGN
Original site: O50320_PORGN 
ID   O50320_PORGN            Unreviewed;       384 AA.
AC   O50320; Q7BW87;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 2.
DT   24-JAN-2024, entry version 113.
DE   SubName: Full=3-amino-5-hydroxybenzoic acid synthase family protein PorR {ECO:0000313|EMBL:SJL31420.1};
DE   SubName: Full=PorR protein {ECO:0000313|EMBL:BAA31964.1};
GN   Name=PorR {ECO:0000313|EMBL:BAA31964.1};
GN   Synonyms=porR {ECO:0000313|EMBL:SJL31420.1};
GN   ORFNames=PGIN_YH522_01198 {ECO:0000313|EMBL:SJL31420.1};
OS   Porphyromonas gingivalis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=837 {ECO:0000313|EMBL:BAA31964.1};
RN   [1] {ECO:0000313|EMBL:BAA31964.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC33277 {ECO:0000313|EMBL:BAA31964.1};
RA   Nakayama K., Ratnayake D.B.;
RT   "Identification, cloning and sequencing of a gene (porR) responsible for
RT   black pigmentation and extrecellular protease production of Porphyromonas
RT   gingivalis.";
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAA31964.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC33277 {ECO:0000313|EMBL:BAA31964.1};
RA   Nakayama K.;
RT   "porR and porS genes of Porphyromonas gingivalis.";
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SJL31420.1, ECO:0000313|Proteomes:UP000188040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SU60 {ECO:0000313|EMBL:SJL31420.1,
RC   ECO:0000313|Proteomes:UP000188040};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; D64132; BAA31964.1; -; Genomic_DNA.
DR   EMBL; FUFI01000027; SJL31420.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50320; -.
DR   PATRIC; fig|837.83.peg.925; -.
DR   OMA; IVNHGMY; -.
DR   Proteomes; UP000188040; Unassembled WGS sequence.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        197
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   384 AA;  42312 MW;  BC7D48EA00F1DD60 CRC64;
     MPTSISQPIV MVDLKKQYLQ MKKQIDEAIH TVIDSTAFIN GKEVHAFAED LAAYLGVKHV
     IPCANGTDAL QISLMALGLK VGDEIIVPDF TYAASAEAIG LLGLTPVFAD VDPITFNLTS
     KGCEKVLSDK TKAIIPVHLF GQSCDMEPLL AFAKRNDLFV IEDNAQAMGG GYTISDGSIR
     KTGTMGHIGC ASFFPSKNLG CYGDGGAVTT NDDELAKRVR MIANHGQKIK YKHDIIGCNS
     RLDTIQAAIL RVKLQYLDRF NALRNEVASH YTSLLEGIEW LQTPTSLQQS SHVYHQYTLK
     LLDQNTRDGL REHLTNHKIA SMIYYPIPLH RQPAFVGIAH WGESLDVSDS LSRTVLSIPI
     YPEMEIEQIH AVVSAIKTFE PSLQ
//
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