ID A4BM65_9GAMM Unreviewed; 396 AA.
AC A4BM65;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=NB231_16323 {ECO:0000313|EMBL:EAR23403.1};
OS Nitrococcus mobilis Nb-231.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Nitrococcus.
OX NCBI_TaxID=314278 {ECO:0000313|EMBL:EAR23403.1, ECO:0000313|Proteomes:UP000003374};
RN [1] {ECO:0000313|EMBL:EAR23403.1, ECO:0000313|Proteomes:UP000003374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nb-231 {ECO:0000313|EMBL:EAR23403.1,
RC ECO:0000313|Proteomes:UP000003374};
RA Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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:EAR23403.1}.
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DR EMBL; AAOF01000001; EAR23403.1; -; Genomic_DNA.
DR RefSeq; WP_005004657.1; NZ_CH672427.1.
DR AlphaFoldDB; A4BM65; -.
DR STRING; 314278.NB231_16323; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_6; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000003374; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:EAR23403.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003374};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EAR23403.1}.
FT DOMAIN 33..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42743 MW; 067B4DE746261EF4 CRC64;
MGIRLAKRVQ RVKPSPTLAV TARAAELRAA GHDIIGLGAG EPDFDTPEHI RAAAVAAIER
GETRYTPVDG TPELKEAIRS KFERENGLHY ELNQIIASSG AKQCLYNLMA AILDPGDEVV
VPAPYWVSYP DMVLLAEGVP EVVEAGQDQR FKLLPEQLEE AITDRTRLVL LNSPSNPSGT
AYTHAELAAL GAVLKRYPEV LIATDDIYEH ILWTTEPFAN IVMLCPELNE RTVIINGVSK
TYAMTGWRLG YAAGPAPVIA AMKKLQSQST SNPSSISQAA AVAALSGDQS CIAPMLRAFK
ERHDYVVERL NSMIGVHCAA GDGTFYCFPS MRGAIRNLDG VNNDIELAEY LIGTAGVALV
PGSAFGLSGH TRISYATSME NLENAMGRLE KVFGCQ
//