ID   A0A136GWA1_9GAMM        Unreviewed;       559 AA.
AC   A0A136GWA1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|ARBA:ARBA00015416};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|ARBA:ARBA00031365};
GN   ORFNames=AXW16_03355 {ECO:0000313|EMBL:KXJ47578.1};
OS   Cycloclasticus sp. Phe_18.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1795870 {ECO:0000313|EMBL:KXJ47578.1, ECO:0000313|Proteomes:UP000070359};
RN   [1] {ECO:0000313|Proteomes:UP000070359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KXJ47578.1}.
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DR   EMBL; LSMQ01000057; KXJ47578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136GWA1; -.
DR   Proteomes; UP000070359; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   559 AA;  63660 MW;  FB80D39CB7AECC8B CRC64;
     MPGDYVLYIA VVFLSFFISI KAYARLKLSR AKHPSLRGHS KWSRRVAKWI PFFSYEDEHF
     FSSDDAPIDV VKQRRDGFNR LSENLKRYSP KSTALYASLE ESVSDVKFTN LYRVPYPYRK
     YIARHIKSAS IVTSSSGVML EDLDGHKGMD LSGSYGVNVF GYDFYKSCLD KGLESAKRLG
     PVLGPYHPLI KDNVEELKRL SGLDEVSFHM SGTEAVMQAV RLARYHTGKR YLVRFCGAYH
     GWWDGVQPGI GNQRKTSDVY TLSDMSERTL GVLRTRKDIA CVLVNPLQGL HPNSDASSDA
     TLIGSGRTAA FDKIAYSEWL QTLQQVCKEQ SIALIFDEVF TGFRLSHKGA QGFFGVQADL
     VTYGKTLGGG LPVGVLCGRH QLMQRFKDDR PVNVSFARGT FNSHPYVLAS MNAFLQAIQA
     ESIQHSYQVL EQVWNDRVKK MNQALEEAGL PIKLANLTSI LTVLYTQPSR YNWMYQYYLR
     NEGLLLSWIG TGRLIMSHNF TDDEFNEVIK RFVVAGIQMK KDGWWWHHSA LTNKWIKRRM
     MKDMMKSLLP TSRANEVKS
//