Q92PZ4

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
KEGG Pathway
sme:SMc01215
EC number
6.3.4.16: Other carbon--nitrogen ligases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

125-211 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q92PZ4

Entry ID Method Resolution Chain Position Source
AF-Q92PZ4-F1 Predicted AlphaFoldDB

No variants for Q92PZ4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q92PZ4

No associated diseases with Q92PZ4

15 regional properties for Q92PZ4

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 203 - 387 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 738 - 801 IPR005479-2
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 828 - 961 IPR005479-3
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 480 - 602 IPR005480
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 631 - 645 IPR005483-1
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 660 - 670 IPR005483-2
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 778 - 790 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 835 - 854 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 869 - 886 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 924 - 953 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 1003 - 1021 IPR005483-7
domain Methylglyoxal synthase-like domain 1027 - 1163 IPR011607
domain ATP-grasp fold 185 - 381 IPR011761-1
domain ATP-grasp fold 743 - 955 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 1033 - 1134 IPR033937

Functions

Description
EC Number 6.3.4.16 Other carbon--nitrogen ligases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKRQDIKSI LIIGAGPIVI GQACEFDYSG TQACKALKEE GYRVILVNSN PATIMTDPGL
70 80 90 100 110 120
ADATYVEPIT PEVVAKIIAK ERPDALLPTM GGQTALNTAL SLRRMGVLDR YNVEMIGAKP
130 140 150 160 170 180
EAIDKAEDRA LFREAMAHIG LETPKSRLAN ATDIKDHDRK SHEAERSALK AKLSGDELDK
190 200 210 220 230 240
ALDELENQWN LGEGDRKQRY VNHAMAIAAQ ALDDVGLPAI IRPSFTLGGT GGGIAYNRSE
250 260 270 280 290 300
FFEIVGSGLD ASPTTEVLIE ESVLGWKEYE MEVVRDKADN CIIICSIENI DPMGVHTGDS
310 320 330 340 350 360
ITVAPALTLT DKEYQIMRNA SIAVLREIGV ETGGSNVQFA VNPENGRLVV IEMNPRVSRS
370 380 390 400 410 420
SALASKATGF PIAKIAAKLA VGYTLDELEN DITGGATPAS FEPSIDYVVT KIPRFAFEKF
430 440 450 460 470 480
PGAEPTLTTA MKSVGEVMAI GRTFAESLQK ALRGLETGLT GLDEIEVPDF DDNGDGRNAI
490 500 510 520 530 540
RAALGTPTPD RLRMVAQALR LGMSEAEVHE ACKIDPWFIA QFKAIVDMEA RIREHGLPAD
550 560 570 580 590 600
AENLRMLKAM GFSDARLATL TGKRPKEVAE LRNALNVRPV YKRIDTCAAE FASPTAYMYS
610 620 630 640 650 660
TYETPFVGAA RSEAQVSDRK KVVILGGGPN RIGQGIEFDY CCCHAAFALK DAGYEAIMIN
670 680 690 700 710 720
CNPETVSTDY DTSDRLYFEP LTAEDVIEIM RAEQENGTLH GVIVQFGGQT PLKLAEALEK
730 740 750 760 770 780
NGIPILGTAP DAIDLAEDRD RFQKLLMKLD LNQPNNGIAY SVEQARLVAG EIGFPLVVRP
790 800 810 820 830 840
SYVLGGRAMQ IIHSESMLQS YLLDTVPGLV PEDIKQRYPN DKTGQINTLL GKNPLLFDSY
850 860 870 880 890 900
LTNAIEVDVD CLCDGKDVFV SGIMEHIEEA GIHSGDSACS LPVHSLGTDM VDELERQTGA
910 920 930 940 950 960
LARALNVGGL MNVQFAIKDG TIYVLEVNPR ASRTVPFVAK TIGAPIAKIA ARVMAGEMLD
970 980 990 1000 1010 1020
EAIAAYGKKP NPRNLKHIAV KEAVFPFARF PGVDTLLGPE MRSTGEVIGL DTDYALAFAK
1030 1040 1050 1060 1070 1080
SQLGAGVDLP RDGTVFVSVR DEDKERVLPA IRILSDIGFK VMATGGTARF LGEQGIVATK
1090 1100 1110 1120 1130 1140
INKVLEGRPH VEDAIRNRQV QLVINTTDGN KAISDSKSLR RATLMQKVPY YTTMAGAEAA
1150 1160
ALAIKALKAG NLEVRPLQSY FET