ID D0LMF1_HALO1 Unreviewed; 468 AA.
AC D0LMF1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=2,4-diaminobutyrate 4-transaminase {ECO:0000313|EMBL:ACY16857.1};
GN OrderedLocusNames=Hoch_4363 {ECO:0000313|EMBL:ACY16857.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY16857.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY16857.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(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; CP001804; ACY16857.1; -; Genomic_DNA.
DR RefSeq; WP_012829455.1; NC_013440.1.
DR AlphaFoldDB; D0LMF1; -.
DR STRING; 502025.Hoch_4363; -.
DR KEGG; hoh:Hoch_4363; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_7; -.
DR OMA; NLMPGVQ; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 50754 MW; CE8ADA034DFD8AB3 CRC64;
MDERAGGLAI PADGRPTLRG QVPGPRSREL LARQAEHESN ARTYPRKLQI GVRRALGSYL
EDVDGNVFID FLSGAGAVPL GHGHPELLAA VHRQAAECTH MLDFPTPIKD AFTRELLSML
PAPMQERMKL QCCGAAGADA VDAAIKLCKT ATGRAEVVSF QGGFHGSTQS TLALTGLRAP
KEPLENLMPG VHFFPYAHCF RCPLALKPDT CSINCVQYLE RALRDENGGV RSPAAVILEL
VQGEGGVIPA QPQFVRELRR ITRELRIPLI VDEIQSGCGR TGTWFAFEHF DIEPDVIVLS
KALGGLGLPI ALILYDRSLD VWGPGAHTGT FRGNQLAFAA SLEMMRVVRR ERILDHVTEE
GAYLRARLEA AQQTVPIMGD VRGLGLMLGV EIVDPRTGRE APRMAAAVQE ALFRRGLLME
LGGRGDCVLR FLPPLNVART TLDAALDILL DTLAHCAAES PLAPEVRA
//