ID V4PII6_9CAUL Unreviewed; 462 AA.
AC V4PII6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:ESQ85200.1};
GN ORFNames=AEAC466_05680 {ECO:0000313|EMBL:ESQ85200.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ85200.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ85200.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ85200.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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}.
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:ESQ85200.1}.
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DR EMBL; AWGE01000005; ESQ85200.1; -; Genomic_DNA.
DR RefSeq; WP_023457168.1; NZ_AWGE01000005.1.
DR AlphaFoldDB; V4PII6; -.
DR STRING; 1282362.AEAC466_05680; -.
DR PATRIC; fig|1282362.3.peg.1137; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000017826; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:ESQ85200.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000017826};
KW Transferase {ECO:0000313|EMBL:ESQ85200.1}.
SQ SEQUENCE 462 AA; 51543 MW; 0B4EFE1C2D9719A1 CRC64;
MYDPHTLSEA DLLALEAQYC SHGDTVHYMD KPRIFTGCEG SYMYDAAGQA YLDLQMWYSA
VNFGYRNPRL NAAAHRQLDT LPQVASQYLH REKIELAALI ARDMEAKFGE KGRVHFNVGG
AQAVEDSLKL VRNASNGKSL MFAFEGGYHG RTLGASAITS SYRYRRRFGH FGDRAQFIEF
PYHFRGPKGV SKEEYGHECV KKFKRLFETE YNGVLDVKTG QCEYAAFYIE PIQGTGGYVV
PPMNFFTELK DVLDQHGVLM VVDEIQMGVY RTGKLWAIEH FGVTPDILVF GKAITNGLNP
LSGLWAKEAL INPGIFPPGS THSTFNANPM GTSVALETLR MVSEEDYGAK VARKGAYFLE
ALKDLQKRWP QIGDVDGLGL ALRCEICQED GFTPNKELLD DMEAEGLKGG IEIDGQTYGL
ILDVGGYYKN VITLAPSLEI TESEIDLAIK LIDALLRRCV NR
//
