ID H0A5T8_9PROT Unreviewed; 441 AA.
AC H0A5T8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:EHL97397.1};
GN ORFNames=HMPREF9946_04193 {ECO:0000313|EMBL:EHL97397.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL97397.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHL97397.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:EHL97397.1}.
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DR EMBL; AGEZ01000163; EHL97397.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A5T8; -.
DR STRING; 1054213.HMPREF9946_04193; -.
DR PATRIC; fig|1054213.3.peg.3814; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_8_0_5; -.
DR BioCyc; ABAC1054213:G1H32-3880-MONOMER; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
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; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
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:EHL97397.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW Transferase {ECO:0000313|EMBL:EHL97397.1}.
SQ SEQUENCE 441 AA; 47364 MW; 5005CB936D9E60EA CRC64;
MTVTMINAFD AKATNGIAPR EQALIERRQK LLGPAYRLFY ANPVHVVRGE GVWLYDPDGN
AYLDVYNNVA SVGHCHPHVV AALSKQAATL NTHTRYINDI ILDYADKLLG YFPPELSHVM
FTCTGSEAND LAYRVARSYT GGTGFIVTQL AYHGVTVAIS EMSPSLGDGI QLGPNVRTIP
APDLYHANGQ DVGEAFAAAV RAAIADMQKA GIKPAALLVD TIFSSDGVFS DPPGFLAPAV
AAIREAGGLF IADEVQPGFG RTGEGMWGFM RHGVVPDMVT MGKPMGNGHP IAGMVAKPEI
LQRFGERTRY FNTFGGNPVS CAVGQAVLEV IENENIIANA RDVGAYLQNG LRDLAKRHEV
IGDVRGAGLF VGVELVKDRE TKAPDGERTA KLVNALRERR VLISAAGPHA NVLKIRPPLV
FQREHADRFL EAADAALAEI G
//
