ID   A0A285NVA1_9AQUI        Unreviewed;       678 AA.
AC   A0A285NVA1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase/spore coat polysaccharide biosynthesis protein SpsF {ECO:0000313|EMBL:SNZ13422.1};
GN   ORFNames=SAMN06265353_0750 {ECO:0000313|EMBL:SNZ13422.1};
OS   Hydrogenobacter hydrogenophilus.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC   Hydrogenobacter.
OX   NCBI_TaxID=35835 {ECO:0000313|EMBL:SNZ13422.1, ECO:0000313|Proteomes:UP000218627};
RN   [1] {ECO:0000313|EMBL:SNZ13422.1, ECO:0000313|Proteomes:UP000218627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2913 {ECO:0000313|EMBL:SNZ13422.1,
RC   ECO:0000313|Proteomes:UP000218627};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBEN01000002; SNZ13422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285NVA1; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000218627; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd02518; GT2_SpsF; 1.
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; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
SQ   SEQUENCE   678 AA;  76869 MW;  CED8E077E4AC5EAB CRC64;
     MTIGIVVQAR TGSTRFPKKI TSKLLGKTVL EWVLLRAGRV GVDKKILATS VLPEDDPVEQ
     IAKSMGWEVL RGSPTDVLSR YAEVVKKFHL NYVVRITGDC PLVDHKLIEF SLEKMTKEDA
     DYITFVGIID GFDVEVINGD WIVIADKLAK LPSEREHVSA YIRKSKKAKK IFLKYHEEDL
     SHIHLSVDYP EDLEVIERIL KELRSEDFTY QDVVRLIKER PELLRRQKQI VPNEGYHKSL
     CEDREFIKGL KGKPLKLEEN LRHFEKTKRL IPNCSQTFSK SYLQFSVGAS PLFVEEGKGA
     YLKDLDGNLY IDYSMGLGAC ILGYAFEPIL EKLQIQLKKG TIYTLPHKLE LELADTLSQI
     IPCAQMVRFG KNGSDVTSVA VRLARAYTGR DMVACCGYHG WQDWYIGTTT LNKGVPKAVK
     NLTLTFEYNN IDSLKKLFDE YQNQIACVIM EPVGVEEPQE GFLLQVKELV HKNGALLIFD
     EVVTGFRFSL GGAQEFFGVV PDIACFGKAM GNGMPISAIV GRRDVMELLE EVFFSFTFGG
     ETLSIASAIA VINFMKEEEV IPYLWEKGTK LKEGITKLIE NKELEELVIV KGYPVRFVLD
     FLGDEALKLK TLFQQECAKR GVLFSGSHNI SYSHTDAEIE KTLQVYDEVL DIVKFAYEYS
     MIDELLEGQV LQPVFRKP
//