ID V4YNL6_9PROT Unreviewed; 405 AA.
AC V4YNL6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=patA {ECO:0000313|EMBL:ESS13242.1};
GN ORFNames=MOLA814_02244 {ECO:0000313|EMBL:ESS13242.1};
OS Betaproteobacteria bacterium MOLA814.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS13242.1, ECO:0000313|Proteomes:UP000017838};
RN [1] {ECO:0000313|EMBL:ESS13242.1, ECO:0000313|Proteomes:UP000017838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS13242.1,
RC ECO:0000313|Proteomes:UP000017838};
RX PubMed=24356832;
RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT Representative of the Betaproteobacteria Common in the Ocean.";
RL Genome Announc. 1:e01062-13(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:ESS13242.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYMW01000003; ESS13242.1; -; Genomic_DNA.
DR AlphaFoldDB; V4YNL6; -.
DR STRING; 1408164.MOLA814_02244; -.
DR PATRIC; fig|1408164.3.peg.2359; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000017838; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:ESS13242.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017838};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ESS13242.1}.
FT DOMAIN 36..401
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 405 AA; 43633 MW; 2D14DA0FA719CB30 CRC64;
MQISQRAQRI KPFMVMEVAK AAQAMAAKTA HTDQPMLFLN IGEPDFSAPL AVQEAAARAM
ANGHTGYTQA LGIAPLRQAI SGWYASRFGL DIDPARIAIT AGASAALQLA CLALVNPGDE
VLMPDPSYPC NRNFVAAADG QAVLLPTTPE QRFQLSAEQI EQAWGDKTRG VLLASPSNPT
GTSIARDELK RVAQTVRAKG GFTIVDEIYL GLNFDEAFSH SALGLEDGLG NDIISVNSFS
KYFNMTGWRL GWLVLPPALV PVVERLAQHL FICASTISQH AALACFQADS LAEFERRRAA
FKARRDYFIP QLNRLGLTVP VVPDGAFYAY ASCEAACQQW GISPGTPEQP GASWTFAFEL
MKRAGIAATP GHDFGGAQNH NFIRFSTASS MEQLVTAVAR LDNAL
//
