ID A7H0H2_CAMC5 Unreviewed; 374 AA.
AC A7H0H2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=UDP-2-acetamido-2, 6-dideoxy-beta-L-arabino-hex-4-ulose aminotransferase {ECO:0000313|EMBL:EAU01464.1};
DE EC=2.6.1.92 {ECO:0000313|EMBL:EAU01464.1};
GN Name=pseC {ECO:0000313|EMBL:EAU01464.1};
GN ORFNames=CCV52592_0561 {ECO:0000313|EMBL:EAU01464.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU01464.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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; CP000767; EAU01464.1; -; Genomic_DNA.
DR RefSeq; WP_011992725.1; NC_009715.2.
DR AlphaFoldDB; A7H0H2; -.
DR STRING; 360105.CCV52592_0561; -.
DR KEGG; ccv:CCV52592_0561; -.
DR HOGENOM; CLU_033332_0_3_7; -.
DR OrthoDB; 5342089at2; -.
DR Proteomes; UP000006380; Chromosome.
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; 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 Aminotransferase {ECO:0000313|EMBL:EAU01464.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW Transferase {ECO:0000313|EMBL:EAU01464.1}.
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 179
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 40847 MW; 247C869999C54299 CRC64;
MIPYSRQSID ESDIAAVVSA LKDDILTGGE KVGEFERAIA EYVGVKHVVA MNSATSALHA
AYLALGVREN DEVITTPITF AATANAALMA GAEVKFCDVK TDGNIDESKI PALITPRTKV
ITAVDFGGNP ANIEQILKLA RERNLKVIDD ASHALGSSLN GAKVGAQADI SIFSFHPVKP
LTTLEGGAIA TNDDELANLA RLYRSHGITK KHLWNSDMSV LGYNYRLSDV ACALGLNQLK
RLDAMIARRG EIAAFYDEKF AKNPYFSTIK IPNGTISSHH LYAILLFPQL WCAKEDIFAA
LHERGIGVQV HYKPTYKFSF YRDRYGETLL PGADEFYNAE LSIPCHQGMS DADAKFVAEN
LLEILAKFDT GCRV
//
