ID K1KF65_9BURK Unreviewed; 423 AA.
AC K1KF65;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN ORFNames=HMPREF9465_02041 {ECO:0000313|EMBL:EKB30374.1};
OS Sutterella wadsworthensis 2_1_59BFAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB30374.1, ECO:0000313|Proteomes:UP000005835};
RN [1] {ECO:0000313|EMBL:EKB30374.1, ECO:0000313|Proteomes:UP000005835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB30374.1,
RC ECO:0000313|Proteomes:UP000005835};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL Submitted (MAY-2012) 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-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:EKB30374.1}.
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; ADMG01000045; EKB30374.1; -; Genomic_DNA.
DR RefSeq; WP_005436753.1; NZ_JH815520.1.
DR AlphaFoldDB; K1KF65; -.
DR STRING; 742823.HMPREF9465_02041; -.
DR PATRIC; fig|742823.3.peg.2041; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_2_4; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000005835; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005835}.
FT DOMAIN 34..395
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 423 AA; 47290 MW; 2562D277E6789EC8 CRC64;
MKLIKKSKKL NNVLYDIRGP IVDRAKEMEA QGQQLIKLNI GNLASFDFQV PEEIQRDMIL
NLPNSAGYSD SKGIFAARKA VMHYTQELGI RGVTLDDIYL GNGASDLISL ATNALLDEGD
ELLIPMPDYP LWTATTSLSG GTPVHYLCDE ENGWQPDLDD IRAKITPRTR GIVIINPNNP
TGAVYPKETL LKLVDIAREF GLIIFADEVY DKILYEDAKH IAIASLSTDV LTITFNSLSK
AYRACGYRAG WMIISGNKLP ARDFIEGLNM LANMKLCANV PGQWAIQTAL GGYQSINDLV
CEGGRLRVQR DLAWELLTQI PGVTCVKPQG SLYMFPRLDP KIYPIENDRQ FFKELLEATR
VLLVQGTGFN WPHPDHFRVV FLPHEPQLRE AISRIAEYLA AWRAAHPVKE EPATPRKKEG
AAE
//