ID   A4G465_HERAR            Unreviewed;       675 AA.
AC   A4G465;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Bifunctionnal protein: Glutamate-1-semialdehyde 2,1-aminomutase, Acylneuraminate cytidylyltransferase {ECO:0000313|EMBL:CAL61302.1};
DE            EC=2.7.7.43 {ECO:0000313|EMBL:CAL61302.1};
DE            EC=5.4.3.8 {ECO:0000313|EMBL:CAL61302.1};
GN   OrderedLocusNames=HEAR1123 {ECO:0000313|EMBL:CAL61302.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL61302.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL61302.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CU207211; CAL61302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G465; -.
DR   STRING; 204773.HEAR1123; -.
DR   KEGG; har:HEAR1123; -.
DR   eggNOG; COG0001; Bacteria.
DR   eggNOG; COG1861; Bacteria.
DR   HOGENOM; CLU_016922_1_5_4; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
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   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; 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.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:CAL61302.1};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:CAL61302.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAL61302.1}.
SQ   SEQUENCE   675 AA;  74941 MW;  1CCFE46D7880E2AC CRC64;
     MKVVALVQAR MGSTRLPDKV MKPIGGVPMI ELLLSRLSRA TEVDQIVVAT SVDVRNLPLV
     EYVHKLGYAC EQGSENDVLD RYVQAARVHQ ADVVVRITGD CPLVDPQLVD EVIRGFKSSN
     TDYFSNISPP TYPDGLDIEV FFLSALEQAS QETDKAYDHE HVTPYLRESG RFKTASMQYP
     EDLSALRWTV DEPADLAVIK NIFQAFSPRT DFSWREVLEL QRQQPAIFHL NQNIIRNEGA
     SMGTGQKLWK RAKQIIPGGS MLLSKRAEMF LPDLWPAYFS KAKGCKVWDL DGNEYIDMSI
     MGIGTNTLGY GHPEVDDAVR RTIDAGNMST LNCPEEVYLA EKLIELHPWA DMARFARSGG
     EANAIAIRIA RAASGKDKVA ICGYHGWHDW YLSANLGDDK VLAGHLLPGL QPNGVPEGLR
     GTVFPFNYNN YAELEALVNE HDIGVIKMEV VRNFGPEDNF LHKVRQLATE RGIVLIFDEC
     TSGFRQTYGG IHKMYGVEPD MAMFAKALGN GYAITATIGR REIMEAAQTT FISSTFWTER
     IGPTAALATL DVMARIKSWE TITNTGLDIT ARWKALAAKY DLSITTNGLP ALTGFGFNSP
     NALAYKTLVT QEMLAKGYLA GTSVYVCTEH TPKVVNDFFE ALEPVFALVK ECEEGRDVMT
     LLKGPVCHSG FKRLN
//