ID A0A0H4WH72_9BORD Unreviewed; 311 AA.
AC A0A0H4WH72;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=AGPR {ECO:0000256|HAMAP-Rule:MF_01110};
DE EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_01110};
DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
DE Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
GN Name=argC_1 {ECO:0000313|EMBL:AKQ56889.1};
GN Synonyms=argC {ECO:0000256|HAMAP-Rule:MF_01110,
GN ECO:0000313|EMBL:AZW17667.1};
GN ORFNames=ACR54_03599 {ECO:0000313|EMBL:AKQ56889.1}, CS347_13270
GN {ECO:0000313|EMBL:AZW17667.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ56889.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ56889.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ56889.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000282741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA Williams M.M.;
RT "Whole genome sequencing of various Bordetella species.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AZW17667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H720 {ECO:0000313|EMBL:AZW17667.1};
RX PubMed=31744907;
RA Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA Unoarumhi Y., Williams M.M., Tondella M.L.;
RT "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT Bordetella Respiratory Pathogens.";
RL mSystems 4:e00702-19(2019).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC {ECO:0000256|HAMAP-Rule:MF_01110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01110};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC Rule:MF_01110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110}.
CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01110}.
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DR EMBL; CP012076; AKQ56889.1; -; Genomic_DNA.
DR EMBL; CP024172; AZW17667.1; -; Genomic_DNA.
DR RefSeq; WP_029581309.1; NZ_LT906461.1.
DR STRING; 103855.ACR54_03599; -.
DR KEGG; bhz:ACR54_03599; -.
DR PATRIC; fig|103855.14.peg.3486; -.
DR eggNOG; COG0002; Bacteria.
DR OrthoDB; 9801289at2; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000036382; Chromosome.
DR Proteomes; UP000282741; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01110; ArgC_type2; 1.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR010136; AGPR_type-2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR NCBIfam; TIGR01851; argC_other; 1.
DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01224; ARGC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01110};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_01110}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01110};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01110}; Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT DOMAIN 5..106
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 117
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 311 AA; 33187 MW; 7612BB91E1FFA8F6 CRC64;
MTQALVFIDG DQGTTGLQIH DRLRGREDLR ILTLPAAERK DSARRAEAIN SCDIAILCLP
DAAAREAVAA IRNPAVRVLD ASSAHRLSEG WEYGFAEWRP GQDGRIATAS RVSNPGCYPT
GAVGLLAPLV AGGWVQADYP VTVHAVSGYS GMGRAGVDEY EGADADKALP YAAYGLGLAH
KHTPEIERYA GLAARPVFTP AYGAYRQGIV LTIALQRRLL PPGVDGAALR ASLERHYAGS
RYVHVVPAEA APERLDPRVA NDSNHLYLHV YENAGHGQIL LAAVYDNLGK GASGAAVQNL
DLMLQGGRPR R
//
