ID Q0BZT4_HYPNA Unreviewed; 311 AA.
AC Q0BZT4;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 135.
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 {ECO:0000256|HAMAP-Rule:MF_01110,
GN ECO:0000313|EMBL:ABI78800.1};
GN OrderedLocusNames=HNE_2314 {ECO:0000313|EMBL:ABI78800.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI78800.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI78800.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI78800.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI78800.1; -; Genomic_DNA.
DR RefSeq; WP_011647307.1; NC_008358.1.
DR AlphaFoldDB; Q0BZT4; -.
DR STRING; 228405.HNE_2314; -.
DR KEGG; hne:HNE_2314; -.
DR eggNOG; COG0002; Bacteria.
DR HOGENOM; CLU_077118_0_0_5; -.
DR UniPathway; UPA00068; UER00108.
DR Proteomes; UP000001959; 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:UP000001959}.
FT DOMAIN 4..105
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 116
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 311 AA; 33475 MW; 65B8550DBF865E86 CRC64;
MLPKVFIDGE AGTTGLQIAE RLKVRTDLEL ISIHADKRKD VDERARLINK ADVVILCLPD
DAARLAVSLV SNPNTVVIDA STAHRVSSGW VYGFAEMDRG QRAIISAAKR ISNPGCYPTG
FVALVRPLVK TGLLPADWPV TVNAVSGYSG GGKPMIAEFE DRETQDNFRI YALGQQHKHP
PEMKKFSGLS HVPMFTPAVG RYAQGMIVEV PLPLWAVPGK PKRKDIHKAL TAAYAGEAFV
KVIPLAEADA IKSLDAEGCN DTNRLEIYVF GTDEQARLVA RLDNLGKGAS GAAVQNLNIA
LGLDEGAGLK V
//
