ID A0A9N9YP52_9HYPO Unreviewed; 1204 AA.
AC A0A9N9YP52;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CRHIZ90672A_00016692 {ECO:0000313|EMBL:CAH0025586.1};
OS Clonostachys rhizophaga.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Bionectriaceae; Clonostachys.
OX NCBI_TaxID=160324 {ECO:0000313|EMBL:CAH0025586.1, ECO:0000313|Proteomes:UP000696573};
RN [1] {ECO:0000313|EMBL:CAH0025586.1}
RP NUCLEOTIDE SEQUENCE.
RA Piombo E.;
RL Submitted (OCT-2021) 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:CAH0025586.1}.
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DR EMBL; CABFNQ020000713; CAH0025586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9YP52; -.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000696573; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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:SF128; UREA AMIDOLYASE; 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 Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal 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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000696573}.
FT DOMAIN 2..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1135..1204
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1204 AA; 132714 MW; 63C20A8A9694172C CRC64;
MELKRVLVAN RGEIAVRLVK ACNKIGITAV AIFVEEDAGS LHVRLADEAY ELSNSDTKGY
LDIDKVVEIC QQHDIQGVIP GYGFLSENTD FARRLQDAGI LFIGPSPESL EEFGLKHRAR
ELAIQAQVPV VPGTPIITTF EEAQEAVRSL GFPVMVKATA GGGGMGLQAC FNLEELEAAV
ETVRSRGTAL FNNAAMFIEK YVQYGRHIEA QIFGNGQGDV VFLGERECSI QRRHQKVIEE
SPSPFVMKNP EIREKMKSAS VLLAKSVKYK SAGTVEFLVD DETGQFYFLE MNTRLQVEHG
VTELCYNVDI VEMMLLQARA ELLSDDRNGG MSLDAFQRDG PAGHAIEVRV YAENPAKDFM
PSPGLLQNVS FPTGSHLRVD TWIETGTNIS PSFDPLLAKV MVHSTTRHGA IDGMQEALRD
SLIQGPPTNM EFLVQILQTA DFQSGYTLTN TLSKRFNYLP NAIEFLSPGA FTSIQDYPGR
VGIPHGVPPS GPMDSLSFRA ANILVGNPEG TEAFEITMTG PVLKFYGDAI LAVCGAQFKM
LLNDEPIATW TRHYIKSGSK LEVLGTQVGA RAYLAILGGL PSIATYLGSK STAPTLNWGG
FQGRCLRAGD FLSLKPLCSQ TGFQPYQVPE VCVPLPERSP GLYALPGPWF SAPFLSPEGQ
AHVFNCEFKL SHNSNRTGMR MQGPPPKWGR DNGGEGGSHP SNMVGFGAPN GSVAFTGDSG
IVYAVDGPDL TGYVVTQVVA QHDLWRLSQL RPGEKFKFTP ITWAQALELE GRVDKFLAAM
KDGSPVPLDW SLPSEEAGDG ILHRSSTFSI RQAGERAILC VFDGDFSVRT RARVEQLARA
FSSAGAPRNL VAGNCSVYVP FDPRAKSQAE MVTSCIELEN GLPSVDEVVL PSRLIYLPAL
FDPRECHEAI ERYMTLQRPS APFLPDNIDF IRRSNGLKTR EDVKEVYFGK PMLVNVVGWL
MGLPIYNPLD PRDHLVVPKF NPSRNWTKAG SLGTGGMSSS IYPNDGPGGH MLWGATIPGL
CWDTYGRKPG FSRGQPWLFR AFDQIIFHEV SREEFDHIVQ RFRREQYEIK IEPAHFDMTA
YRRLMKEVGS ELESLRVLRQ KCTQIELEAE EKLYKEWEVS RQKANDVTIA EDENLIKVSI
DTTSNVWKIN VQVGDIVKQG DVVVVLEAMK MEITVRSPAA GKVEAVLKNP GDLAEAGDTI
MLLR
//
