ID Q0A7M0_ALKEH Unreviewed; 407 AA.
AC Q0A7M0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Mlg_1823 {ECO:0000313|EMBL:ABI57167.1};
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272 {ECO:0000313|EMBL:ABI57167.1, ECO:0000313|Proteomes:UP000001962};
RN [1] {ECO:0000313|Proteomes:UP000001962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1
RC {ECO:0000313|Proteomes:UP000001962};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000453; ABI57167.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0A7M0; -.
DR KEGG; aeh:Mlg_1823; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_6; -.
DR Proteomes; UP000001962; 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; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 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 ECO:0000313|EMBL:ABI57167.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001962};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABI57167.1}.
FT DOMAIN 34..370
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 407 AA; 45950 MW; 2FC077E0893C8360 CRC64;
MNLSDEFPRI KRLPPYVFNI VNELKAAARA RGEDIVDFGM GNPDQPTPQH IVDKLTEVAQ
RGDTHRYSMS RGIPRLRRAI CNWYRDRYDV DLDRETEAIV TIGSKEGLAH LALATLAPGD
AVLVPNPAYP IHPYGVVIAG ADIRHVPMLP DGDFFAEMEK AIRDSYPKPK MLILNFPSNP
TSACVDLEFF EKVVAVARQH NIWVVHDLAY ADIVFDGYRA PSILEVPGAK EVAVESFSLS
KSYNMPGWRV GFMCGNRHLI AALARMKSYL DYGTFTPIQV AAIAALEGPQ ECVQEICEMY
RRRRDVLCEG LNAAGWEVEK PKATMFVWAR IPERYRDMGS LEFAKKLLRD AKVAVSPGIG
FGDYGDEYVR FGLIENEHRT RQAIRCIKQM FRRDGQHDQQ QEGEVSS
//
