ID A0A1D7XT79_9FLAO Unreviewed; 437 AA.
AC A0A1D7XT79;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:AOR26380.1};
GN ORFNames=FORMA_12180 {ECO:0000313|EMBL:AOR26380.1};
OS Formosa sp. Hel3_A1_48.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR26380.1, ECO:0000313|Proteomes:UP000094318};
RN [1] {ECO:0000313|EMBL:AOR26380.1, ECO:0000313|Proteomes:UP000094318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR26380.1,
RC ECO:0000313|Proteomes:UP000094318};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP017259; AOR26380.1; -; Genomic_DNA.
DR RefSeq; WP_069674775.1; NZ_CP017259.1.
DR AlphaFoldDB; A0A1D7XT79; -.
DR STRING; 1336795.FORMA_12180; -.
DR KEGG; foh:FORMA_12180; -.
DR PATRIC; fig|1336795.4.peg.1166; -.
DR Proteomes; UP000094318; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AOR26380.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000094318};
KW Transferase {ECO:0000313|EMBL:AOR26380.1}.
SQ SEQUENCE 437 AA; 48946 MW; 3329D3CD08AB84FA CRC64;
MNNRTGQNLY KKAKTLIPGG TMLLSKRPEM FLPDNWPSYF SKAKGCKVWD LDGKEYTDMC
IMGIGTNTLG YGNDEVDNAV IETVKKGNMS TFNCPEEVAL AEKLVELNPW ADMVRFARSG
GEANSIAIRI ARAASGKDKV AICGYHGWHD WYLSANHNKG DDLSNHLLSG LNPNGVPKNL
KNTVYPFHYN DFEELLSIVN QNDIGVIKME VMRNFGPRDN FLQKVRDLAT QRNIVLIFDE
CTSGFRETYG GIYKKYGVEP DVAMYGKTIG NGYALTAVVG KKSVMEAAQT SFISSTFWTE
RIGPTAALKT LEVMYKMSSW DIITDQGKKI QNQWKSLAET HNLSISVSGM PALSTYSFNS
ENAMEYKTFI AQEMLKKGFL ASTNFYACTE HKDDQIVDYF DALDGVYKMI SDCEKGQKNI
QDLLEGPVCH SGFKRLN
//
