ID E1SVK1_FERBD Unreviewed; 466 AA.
AC E1SVK1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADN75347.1};
GN OrderedLocusNames=Fbal_1138 {ECO:0000313|EMBL:ADN75347.1};
OS Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN75347.1, ECO:0000313|Proteomes:UP000006683};
RN [1] {ECO:0000313|EMBL:ADN75347.1, ECO:0000313|Proteomes:UP000006683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC {ECO:0000313|Proteomes:UP000006683};
RX DOI=10.4056/sigs.1161239;
RA Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL Stand. Genomic Sci. 3:174-182(2010).
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; CP002209; ADN75347.1; -; Genomic_DNA.
DR RefSeq; WP_013344653.1; NC_014541.1.
DR AlphaFoldDB; E1SVK1; -.
DR STRING; 550540.Fbal_1138; -.
DR GeneID; 67181373; -.
DR KEGG; fbl:Fbal_1138; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_1_6; -.
DR Proteomes; UP000006683; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:ADN75347.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006683};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADN75347.1}.
SQ SEQUENCE 466 AA; 50643 MW; B8C2203EBC187888 CRC64;
MPAMTKDIDM TQNPNAQTQA WQQLDAAHHL HPFTDNGALN AKGSRVISHA DGVYIHTPEG
DAILDGMAGL WCVNMGYGRT ELVQAATEQL NTLPYYNLFF QCTHPPATEL AAQLTSLLPD
HLNRVFFTGS GSECNDTVVR MVRHYWASQG QPKRKAIISR HNAYHGSTMA GASLGGMKPM
HAQGGLPIPD IHHIDQPYHF GEGQGMDANE FGLERARQLE AKILELGPEN VAAFIGEPVQ
GAGGVIIPPE TYWPEVQRIC RQYDILLISD EVICGFGRLG HWLGCEHFGV KPDLVCMAKG
ITSGYVPLGA VAVGDRVAQG LLDNGGDFNH GFTYSGHPVA CAVASANLKL MADEKVLERI
NEHTAPYLQR RWAELADHPL VGEARGLGMV AALELVADKA SGKRFDENVG AGTVCRDFCI
ESGLVMRAVG DTMIISPPLI ITEAEIDELI ARARRSLDLT WQKLVG
//
