ID I4WCY8_9GAMM Unreviewed; 374 AA.
AC I4WCY8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glutamate--GDP-4-keto-6-deoxy-D-mannose aminotransferase {ECO:0000313|EMBL:EIL97329.1};
GN ORFNames=UU5_05426 {ECO:0000313|EMBL:EIL97329.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL97329.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL97329.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL97329.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, 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:EIL97329.1}.
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DR EMBL; AJXS01000134; EIL97329.1; -; Genomic_DNA.
DR RefSeq; WP_008210259.1; NZ_AJXS01000134.1.
DR AlphaFoldDB; I4WCY8; -.
DR PATRIC; fig|1162282.3.peg.1034; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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 Aminotransferase {ECO:0000313|EMBL:EIL97329.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:EIL97329.1}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 41023 MW; 0992FED10D5D21C8 CRC64;
MNTEPPSRIY YTKPSITALE IGYANDAASN GWGEHCYDYI HRFEAMFREH LGVKHAIATS
SATGALHIGM AAMGIGAGDE VVLGDINWVA SAAPIIHLGA TPVLVDVLAD SWCLDPVAVE
AAITPKTRAI LAVHLYGNLC DMDVLREIGE RHGIPVIEDA AEAIGSVWHG CRAGSMGIFG
AFSFHGTKTI TTGEGGIFVT NDDALYEKAL TLSNHGRARE ETRQFWPATI GFKYKMSNLQ
AAIGCGQMER IEELIAGKRR VFEYYCNALR MLPLRMNPEP AGTINGYWMP TIVVDDHALF
DRDALLDAFK ANHIDGRVFF WPLSSLPSFK PRPENIVSHS LSSRAMNLPS YHDMTDEGQN
RVITCVNKLL ALES
//
