ID U2UPQ5_9FIRM Unreviewed; 395 AA.
AC U2UPQ5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF1985_00860 {ECO:0000313|EMBL:ERL05107.1};
OS Mitsuokella sp. oral taxon 131 str. W9106.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL05107.1, ECO:0000313|Proteomes:UP000016614};
RN [1] {ECO:0000313|EMBL:ERL05107.1, ECO:0000313|Proteomes:UP000016614}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9106 {ECO:0000313|EMBL:ERL05107.1,
RC ECO:0000313|Proteomes:UP000016614};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERL05107.1}.
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; AWVT01000009; ERL05107.1; -; Genomic_DNA.
DR RefSeq; WP_021771128.1; NZ_KI273057.1.
DR AlphaFoldDB; U2UPQ5; -.
DR STRING; 1321781.HMPREF1985_00860; -.
DR PATRIC; fig|1321781.3.peg.817; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_9; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000016614; 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; 3.90.1150.10; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383:SF5; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000016614};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 34..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 395 AA; 44099 MW; EFEF14CE246FEAFA CRC64;
MIESRDWSSR LSPSVQSIAP SGIRKFFDIA AQMKDVISLG VGEPDFITPW TIRESCVYGL
ECGYTSYTAN RGMMELREEI AYHYEQEYET RYDPATDILV TVGVSEALDL AMRAVLATGD
EVLIPEPCYV SYQACTILAG GVPVSVPTKL ENEFRITPDE LEQYVTDRTR VLLIGYPNNP
TGAVMERADL LAIAKFAEKH DLLVISDEIY GDLTYGDEKH IAFSSLPNMQ ERTILLNGFS
KAYAMTGWRI GYAMGNQAII AAMTKIHQYT MLCAPITAQL AAIEALRRGE KYMKKMVAEY
DRRRRLIYDG FTKIGLPCFE PKGAFYIFPD ITPSGYQDEE FAEELLKAEH VALVPGSAFG
VCGAGHVRCS YATSIDKISE ALARIENFLA KHKKT
//
