ID A3YCJ4_9GAMM Unreviewed; 452 AA.
AC A3YCJ4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 03-MAY-2023, entry version 65.
DE SubName: Full=Carbamoyl-phosphate synthase, putative {ECO:0000313|EMBL:EAQ65116.1};
GN ORFNames=MED121_10360 {ECO:0000313|EMBL:EAQ65116.1};
OS Marinomonas sp. MED121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ65116.1, ECO:0000313|Proteomes:UP000003436};
RN [1] {ECO:0000313|EMBL:EAQ65116.1, ECO:0000313|Proteomes:UP000003436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED121 {ECO:0000313|EMBL:EAQ65116.1,
RC ECO:0000313|Proteomes:UP000003436};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ65116.1}.
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DR EMBL; AANE01000008; EAQ65116.1; -; Genomic_DNA.
DR RefSeq; WP_009834376.1; NZ_CH672431.1.
DR AlphaFoldDB; A3YCJ4; -.
DR STRING; 314277.MED121_10360; -.
DR HOGENOM; CLU_000395_3_2_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000003436; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
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}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 452 AA; 49856 MW; A5BCB99184E871F3 CRC64;
MKKILIANRG EIACRVIKSC QKLGIKTVAV YSSADENALH VEMADEAFHI GPAKASESYL
QAHKILEVCQ LAHVDAVHPG YGFLSENTEF ARLLEQNGII WIGPSAKSIL DMGDKERARS
LAVYAGVNVL PGSRRFTLDD HNGLLEAAEV VGFPLLVKAS AGGGGIGMRL VESAQNLAQT
VESTQQMAAR SFGDGTIFME RYVAKARHIE IQVFGFGNGR AIHLYERECS IQRRFQKIIE
EAPAPGIPTA IRDDMAAAAV RLTQEQNYLG AGTVEFILDA DTFEYFFLEM NTRIQVEHPV
TEMTTNTDLV SMQIQLAFGE DLSHITQDSI AQQGHAIEAR IYAEDPSRMF LPCPGVINQF
QLTTDNPDIR LDTGIRSGDK ITAYYDPMIA KLICFGAERE VAIKTLDKSL KEASLEGIKN
NISFLINTLN HSEFNEGRSF TGFIDAYKSE LI
//
