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Database: UniProt
Entry: A0A109QZ13_9MICO
LinkDB: A0A109QZ13_9MICO
Original site: A0A109QZ13_9MICO 
ID   A0A109QZ13_9MICO        Unreviewed;       437 AA.
AC   A0A109QZ13;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=GntR family transcriptional regulator {ECO:0000313|EMBL:AMB59865.1};
GN   ORFNames=AWU67_14480 {ECO:0000313|EMBL:AMB59865.1};
OS   Microterricola viridarii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microterricola.
OX   NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB59865.1, ECO:0000313|Proteomes:UP000058305};
RN   [1] {ECO:0000313|EMBL:AMB59865.1, ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB59865.1,
RC   ECO:0000313|Proteomes:UP000058305};
RX   PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA   Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT   isolated from Sikkim Himalaya.";
RL   J. Biotechnol. 222:17-18(2016).
RN   [2] {ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA   Kumar R., Singh D., Swarnkar M.K.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT   Sikkim Himalaya.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP014145; AMB59865.1; -; Genomic_DNA.
DR   RefSeq; WP_067230590.1; NZ_CP014145.1.
DR   AlphaFoldDB; A0A109QZ13; -.
DR   KEGG; mvd:AWU67_14480; -.
DR   OrthoDB; 199743at2; -.
DR   Proteomes; UP000058305; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProt.
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; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000058305}.
FT   DOMAIN          59..400
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   437 AA;  47780 MW;  E0AD412B993E9754 CRC64;
     MTENNQPGNN LDPWYSHYAE RAAGLRASEV RALFAVASRP EVVSLAGGMP FVSALPQDLV
     INAMDQVMVK QGPTALQYGS GQGVPALREQ ILEVMALEGI QANADDIVVT TGSQHALELV
     SKLFLDPGDV VISEGPSYVT AMVIFRSYQA DVDHVPMDEH GMIPEALREH ITRLKAAGRN
     IKLLYTIPSF HNPAGVTLSW ERRIEILAIA KEHNILVLED NPYGLLYFDK PAPDAMRSIE
     EEGVIYLGTF SKTLAPGFRT GWALAPHAIR EKLVLANEAA VLSPSSFSQL VISEYLATAD
     WKEQINTFRG VYRERKEAMI SALGEHLPQL EWTNPNGGFY VWVTLPEPLD SKAMLPRAVK
     ELVAYTPGTA FYGDGNGHQN MRLSFCYPTP EQIRLGIRRL ASVIGGELEL LETFKGTGTL
     GAAPGTAQFA SPPPNVS
//
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