ID A0A1F7X838_9BACT Unreviewed; 371 AA.
AC A0A1F7X838;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Z22_01800 {ECO:0000313|EMBL:OGM11206.1};
OS Candidatus Woesebacteria bacterium RBG_16_34_12.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802480 {ECO:0000313|EMBL:OGM11206.1, ECO:0000313|Proteomes:UP000177053};
RN [1] {ECO:0000313|EMBL:OGM11206.1, ECO:0000313|Proteomes:UP000177053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM11206.1}.
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DR EMBL; MGFS01000024; OGM11206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7X838; -.
DR Proteomes; UP000177053; Unassembled WGS sequence.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 179
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 371 AA; 41668 MW; E81516B81ACCE866 CRC64;
MPLAKPYFDL EELEEIRKVL DSGWVSQGPK VKEFEDKIAS YLGVKYAIAV TNCTAALHLA
LLSCGIKKGD EVLVADFTFP ATGHSVLYCG ARPVFADVKL NTYNIDTELI EEKITDKTKA
IIPVHTFGQP AEMDKIIEIS KNYNLKVIED AACALGAKYN GKYAGTIGDI GCFSFHARKG
ITTGEGGMAV TNDKDLAEKM RHLSVFGMTS AWVREKSDEF VVPKFTEAGY NYKMSDITAA
VGVAQLRKLD KIIERKTVLA KYWNEKLQEI ELIEPPYVDN NVKHVYQSYV SLVDKRINRN
KIIESLMKKD VQTQIGTYAS HIQPVYNSTD TCSNSFEIFE RSLALPMYFT LREEDIDMVA
KHLKTALEEL K
//