ID   I0HT91_RUBGI            Unreviewed;       323 AA.
AC   I0HT91;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:BAL96228.1};
GN   OrderedLocusNames=RGE_28890 {ECO:0000313|EMBL:BAL96228.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL96228.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL96228.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA   Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT   gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000256|ARBA:ARBA00005011}.
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DR   EMBL; AP012320; BAL96228.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0HT91; -.
DR   STRING; 983917.RGE_28890; -.
DR   KEGG; rge:RGE_28890; -.
DR   PATRIC; fig|983917.3.peg.2817; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_2_4; -.
DR   Proteomes; UP000007883; 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); 2.
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; PTHR43643:SF6; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:BAL96228.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW   Transferase {ECO:0000313|EMBL:BAL96228.1}.
FT   DOMAIN          23..316
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   323 AA;  33873 MW;  5FD203A072E7AB5F CRC64;
     MHGGPDRHGP APWDFSTCAN AAGPCPAAVA ALQRVDPTRY PDSGYHALRE RLAAWHRVTP
     ERIVLAASAS EFIQRITTVG TRLAPGAVAL PPHAYGDYAA AAQANGRACT RLGDPRASLR
     WLGEPSSPLG QDTPPPPDLA RVPTVLDSVY APLRLGGASR WATADRQAVF VLHGPNKALG
     LCGLRGAYAI APDADAVDWD LGAWTAALAA AEPSWPLGAH AVAMLEIWTE AATQRWLAGA
     RLTLGEWLAG LRVALEELGF ETLPSVANFL CVRPPPGAPD AASLRRHGVA VRDTGSFGLP
     GHWRLSAQPP ATVAALRAAL RGG
//