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
//