ID K4IKZ6_PSYTT Unreviewed; 950 AA.
AC K4IKZ6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Carbamoyl-phosphate synthase large chain CarB {ECO:0000313|EMBL:AFU70463.1};
GN OrderedLocusNames=P700755_003890 {ECO:0000313|EMBL:AFU70463.1};
OS Psychroflexus torquis (strain ATCC 700755 / ACAM 623).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU70463.1, ECO:0000313|Proteomes:UP000008514};
RN [1] {ECO:0000313|EMBL:AFU70463.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFU70463.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Feng S., Powell S.M., Bowman J.P.;
RT "The complete sequence of Psychroflexus torquis an extreme psychrophile
RT from sea-ice that is stimulated by light.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CP003879; AFU70463.1; -; Genomic_DNA.
DR RefSeq; WP_015025997.1; NC_018721.1.
DR AlphaFoldDB; K4IKZ6; -.
DR STRING; 313595.P700755_003890; -.
DR KEGG; ptq:P700755_003890; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_2_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000008514; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 134..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 688..879
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 950 AA; 106092 MW; AF0EF8D3414C97AC CRC64;
MPKNNSIKTI LLIGSGPIVI GQACEFDYAG SQSLRSLREE GIKTILINSN PATIMTDPSM
ADHVYLKPLT TKSIVDILNA HPDIDAVLPT MGGQTALNLC IEADDKGIWE DFGIKIIGVD
IDAINITEDR EKFRKLMQHI GIGVAPSKTV TSFLQGNEVA QDFGFPLVIR ASFTLGGSGA
SIVYSEDSFE ELLTRGLEAS PIHEVIIDKA LIGWKEYELE LLRDRNDNVT IICSIENMDP
MGIHTGDSIT VAPAMTLSDR TYQKMRDMAI KMMRSIGDFA GGCNVQFAVS PDEKEDIIAI
EINPRVSRSS ALASKATGYP IAKVASKLAI GYHLNELHNQ ITQTTSAFFE PTLDYVIVKI
PRWNFDKFEG SDRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKSYTDY
NQILSKLEYA SWDRVFVIYD AIQLGIPLSR IHEITKIDMW FLKQYEELYS LEKEISKYDI
KSITKELMLE AKQKGFADRQ IAHMLKCLES EVYTKREELN VNRIYKLVDT CAAEFEAKTP
YYYSTFEADV IDANGEKVLA NESVVTDKKK VIVLGSGPNR IGQGIEFDYC CVHGVMAAAE
CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIK HENPEGVIVQ LGGQTALKLA
EKLSRYGVKI LGTSFESLDL AEDRGSFSKL LQQNNIPYPE FGVAETADEA LALAEELDFP
ILVRPSYVLG GQGMKIVINK KELETHVVDL LMKMPNNKLL LDHYLDGAIE AEADAICDGE
DVYIIGIMEH IEPCGVHSGD SNALLPPFNL GDLVLEQIKD HTKKIALSLN TVGLLNVQFA
IKDDNVYIIE ANPRASRTVP FIAKAYKEPY VNYATKIMLG HKKVKDFNFN PQLEGYAIKQ
PVFSFDKFHN VNKQLGPEMK STGESILFID SLKDDTFYEL YGRRKMYLSK
//
