ID G0J0K1_CYCMS Unreviewed; 437 AA.
AC G0J0K1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:AEL23917.1};
GN OrderedLocusNames=Cycma_0133 {ECO:0000313|EMBL:AEL23917.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL23917.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) 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; CP002955; AEL23917.1; -; Genomic_DNA.
DR RefSeq; WP_014018216.1; NC_015914.1.
DR AlphaFoldDB; G0J0K1; -.
DR STRING; 880070.Cycma_0133; -.
DR KEGG; cmr:Cycma_0133; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_10; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000001635; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AEL23917.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001635};
KW Transferase {ECO:0000313|EMBL:AEL23917.1}.
SQ SEQUENCE 437 AA; 48161 MW; 5CF5B7D2B73C40C3 CRC64;
MTTEKYQKSA DLLARAKNVL AGGVSSEFRK YNHPHALFYS HGSGSRIYDV DGNEYRDFTL
SQGPLILGHS HPEVLKAVHD YSSKGQLFAG QHIMELELAE KLQELIPSAE MMRFCLDGSE
AVQTAFRVAR SKTGKSKFLR FEGHYHGWLD NVCFGISTPS PEALGPRKAP TPSPWSQGLP
PDAINEFHLL PWNDLDLVKA KLAESHHEIA AIITEPIMCN NGCIVPKEGF LQGLRELCDE
YNIALIFDEV ITGFRIGLKG AQTYFGITPD MSIFAKAIGS GYPISAIVGK KEWMEEISSA
RVIHAGTMNT ANPTVAAAMA TVSVLEREDP YAKMFELGDQ LRAGLKEIAK KTGHNMIVSG
IGPIIHTGFS DGEALSEFRD VLKLDKAKLG QFISGLHDDG VRVIGRGLWY LSAVHTEEDI
LFALKSVEKV LMKMNEK
//
