ID A0A1X2HHM8_SYNRA Unreviewed; 704 AA.
AC A0A1X2HHM8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP binding domain-domain-containing protein {ECO:0000313|EMBL:ORY97946.1};
GN ORFNames=BCR43DRAFT_457179 {ECO:0000313|EMBL:ORY97946.1};
OS Syncephalastrum racemosum (Filamentous fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY97946.1, ECO:0000313|Proteomes:UP000242180};
RN [1] {ECO:0000313|EMBL:ORY97946.1, ECO:0000313|Proteomes:UP000242180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY97946.1,
RC ECO:0000313|Proteomes:UP000242180};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:ORY97946.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCGN01000004; ORY97946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2HHM8; -.
DR STRING; 13706.A0A1X2HHM8; -.
DR InParanoid; A0A1X2HHM8; -.
DR OMA; FVEICSH; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000242180; 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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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 SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000242180}.
FT DOMAIN 31..478
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 150..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 628..703
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 704 AA; 78048 MW; 891152F2454C97E4 CRC64;
MFRLCTQYNT KPWRFSLSAR HAYSTQARNT LFEKILIANR GEIACRVMRT AKKLGIKTVA
VYSEADANAQ HVKMADEAFL IGPPPSAQSY LSIDKILNVA RMTGSQAIHP GYGFLSENAE
FADRVTAEKL AFIGPSGDAM RSMGSKSESK FIMEDAGVPV VPGYHGENQD VKFLKEQADK
IGYPVLIKAV KGGGGKGMRI VRSPSEFEEM LESSKNESIK SFGDDKVLVE KYLERPRHVE
VQVFADKHDN VVHLFERDCS VQRRHQKVIE EAPGPGLTEE IRAQLGAKAV AAARAVGYEN
AGTVEFIMDN VDKQFYFMEM NTRLQVEHPV TEMVTNTDLV HWQLEVASGN RLPMTQEELR
LMGHAFEARI YAENPSNHFL PDTGTLFSVR TPEPSEDVRV ETGFIQGDQI SVHYDPMIAK
LVVRGEDRNE ALRRFRRALE QYQIVGLNTN IDFVKRVAEH PEFIKGEVET GFIQQFEKDL
LKPAETPSPL TLATAANGLL LQEYARIQVS QKDPFSPWST LHSNFRLNGK DPREFTFISS
HGEHKVAVTP SQQAGSVDIT VTLGQDQAPT TYTNVSSHWT DDGQVVSSID DKKVKSNVVT
KGEKVTVFDE AGRTDLTLPT PGYILASAAG VAGTGSVKTP MPCKISQVLV KPGQQVEKDT
TLIVLEAMKM EHVIKAPMAG TIDQVLYAVG DLVDENKNLV TFAE
//