ID A6VMF6_ACTSZ Unreviewed; 404 AA.
AC A6VMF6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN OrderedLocusNames=Asuc_0783 {ECO:0000313|EMBL:ABR74153.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74153.1, ECO:0000313|Proteomes:UP000001114};
RN [1] {ECO:0000313|Proteomes:UP000001114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC {ECO:0000313|Proteomes:UP000001114};
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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}.
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DR EMBL; CP000746; ABR74153.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VMF6; -.
DR STRING; 339671.Asuc_0783; -.
DR KEGG; asu:Asuc_0783; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_2_6; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000001114; Chromosome.
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; 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 Aminotransferase {ECO:0000313|EMBL:ABR74153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW Transferase {ECO:0000313|EMBL:ABR74153.1}.
FT DOMAIN 35..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 404 AA; 45448 MW; FEB2D065130A7942 CRC64;
MTFFPKSDKL EHVCYDIRGP VHQEALRLEE EGNKILKLNI GNTAAFGFEA PDEVLVDIMR
NIATSQGYCD SKGLYSARKA IVQYYQSKGI MGATVNDVYI GNGASELITM AMQALLNNDD
EVLVPMPDYP LWTAAVTLAG GKAIHYLCDE EQDWFPSVED IKSKVTSRTK AIVIINPNNP
TGAVYSKELL QDIVEVARQN GLLIFADEIY DKITYDDAVH YHIAALAPDL LTITLNGLSK
AYRVCGFRQG WMILNGPKAQ AKGYIEGLDM IASMRLCANV PMQHAIQTAL GGYQSINEFI
VPGGRLYDQR ERAYQLLNDI PGVSCVKPKG ALYMFPKIDI ERFNIYDDEK MVLDLLRQEK
VLLVHGRGFN WHKPDHFRLV FLPHIQTLED ALGKFARFLS TYRQ
//