ID Q5NMQ4_ZYMMO Unreviewed; 446 AA.
AC Q5NMQ4;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 2.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:AAV90006.2};
GN OrderedLocusNames=ZMO1382 {ECO:0000313|EMBL:AAV90006.2};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV90006.2, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV90006.2, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; AE008692; AAV90006.2; -; Genomic_DNA.
DR RefSeq; WP_011241166.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NMQ4; -.
DR STRING; 264203.ZMO1382; -.
DR KEGG; zmo:ZMO1382; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_8_0_5; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAV90006.2};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001173};
KW Transferase {ECO:0000313|EMBL:AAV90006.2}.
SQ SEQUENCE 446 AA; 48700 MW; B1EF89B7C5E3657D CRC64;
MSSRSTIMDT NSFRDEHAAA LDEATRSLTE RRKDLLGASY RLFYRRPVHL VRGKGAYLWD
ANGDKYLDVY NNVASIGHCH PAVIEAVYEQ MSRLNTHTRY LHETILDYSE AILATMPEEI
NRAMYMCTGS EANDLAMRIA CEWSGGTGII VTQESYHGTS FLTSGASPAL GSGQNLSTNT
RLVPAPDHYR LAGQDAGAWF AAEMQKQIDD MAAHGIKFAG FMADSIFSSD GVLPGEAGFL
KEAIDVVHKN GGIFIADEVQ PGFVRTGESF WGFGRHGLIP DVVTTGKPMG NGIPVSGLFA
RKEVMEAFSN HVPYFNTFGG NPVSMAAASA VLNVIKEENL QTHTQKVGAE LLGELKKLQD
KHESVGDVRG AGLFIGFELV KDRNSKEPDK ELALDLIETL RDEHVLTSVA GPYGNVLKLR
PPLAFQSGDI DWLTGALDRS LTKLGR
//
