ID A0A2M8GY97_9VIBR Unreviewed; 390 AA.
AC A0A2M8GY97;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:PJC86297.1};
GN Name=pseC {ECO:0000313|EMBL:PJC86297.1};
GN ORFNames=CSW98_08750 {ECO:0000313|EMBL:PJC86297.1};
OS Vibrio sp. HA2012.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1971595 {ECO:0000313|EMBL:PJC86297.1, ECO:0000313|Proteomes:UP000232179};
RN [1] {ECO:0000313|EMBL:PJC86297.1, ECO:0000313|Proteomes:UP000232179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA2012 {ECO:0000313|EMBL:PJC86297.1,
RC ECO:0000313|Proteomes:UP000232179};
RA Wang K.;
RT "The draft genome sequence of Vibrio sediminis HA2012.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:PJC86297.1}.
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DR EMBL; PFXK01000004; PJC86297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8GY97; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000232179; 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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000232179}.
FT ACT_SITE 192
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 192
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 390 AA; 43664 MW; 297D5F6488F744AC CRC64;
MSNKVIPYGR QEITQQDIDG VVEVLQSDFL TQGPKVPEFE KALMNQTGAT HALAVNSATS
ALHIACLALG LGEGDWLWTS PITFVASANC GLYCRAKVDF VDIDPNTYNM CPVKLEQKLV
EAKAKGTLPK VVVPVHLCGQ PCDMKAIGKL AKEYGFKVIE DASHAIGGQY HGQPIGNCEY
SDITVFSFHP VKIVTTAEGG AALTNQSELA ERMALFRSHG VTRDPALIEG ESHGGWYYQQ
VELGYNYRMT ELQAALGVTQ MQRLERFVSA RHKLAKRYNE LLKDLPVTVP YQLENTYSGL
HLYVIRLQLD NIVLSHREVF ELLRERGVGV NLHYIPVHTQ PYYQRMGFKQ GDFPESERYY
QEAISLPIFH SMSLEQQDTV VKVLSDILAR
//
