ID Q0EY79_9PROT Unreviewed; 1199 AA.
AC Q0EY79;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Allophanate hydrolase subunit 2 {ECO:0000313|EMBL:EAU54313.1};
GN ORFNames=SPV1_06114 {ECO:0000313|EMBL:EAU54313.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU54313.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU54313.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU54313.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., 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 (SEP-2006) 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:EAU54313.1}.
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DR EMBL; AATS01000010; EAU54313.1; -; Genomic_DNA.
DR RefSeq; WP_009851516.1; NZ_DS022295.1.
DR AlphaFoldDB; Q0EY79; -.
DR STRING; 314344.AL013_02645; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_002162_0_1_0; -.
DR InParanoid; Q0EY79; -.
DR OrthoDB; 5298467at2; -.
DR Proteomes; UP000005297; 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 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; 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; 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 InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
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 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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAU54313.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000005297}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1118..1195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1199 AA; 131898 MW; C80FC1DF1B83AB53 CRC64;
MFSKVLIANR AAIACRIGRT LNQMGIESVG LYTRADSTSR HVAMLDEAIC IGESSASDTY
LNIDKVIQAA LDTGAQAIHP GYGFLSENVA FAEACEKNGI RFVGPTPEQL SCFGLKHTAR
QIAKEQQVPL LPGTELLLDL DEAVAAAESI GYPVMLKSTA GGGGIGMQLC WKAEDLVSAF
ESVKRLGRSN FSNDGVFLEK YIEHARHIEV QIFGDGKGFV TALGERDCST QRRNQKVLEE
SPAPNISDAV RAAMMDTAVR LGEAVEYRSA GTVEFIYDPN SESFYFLEVN TRLQVEHGVT
EEVTGVDLVE WMIRLAAGES AFIRDYRHAP VGHAIQARIY AEDPGKEFRP SAGMINHVVL
PGKTRFDTWI AAGVEVPPYY DPMLGKLIVK AASREEAVEH LSAALHHTAI AGVETNLNYL
RQVVVDDQFI EGRAYTRYLN SFVYEEHSIE VLNAGTQSML QDYPGRLGYW DVGVPPSGPI
DNYAFRLGTR LLGNDENAAG LEITVSGPTL KFNADSVFAL TGARMKATLN GAAVPFWQAV
AVKAGDVLKI GAVEDAGQRS YLCVAHGFQV PDYLGSKSTF TLGGFGGHCG RALRVGDKLH
IKPALPAGDE PALPAALIPG QDEHLHIRVL YGPHGAPDFF TDADIEMFFA TDWEVHYNSS
RTGVRLVGPR PAWARSDGGE AGLHPSNIHD NAYAVGTIDF TGDMPIILGP DGPSLGGFVC
PATIIKADLW KMGQLKPGDR VRFIAVDEAT AVVLEKEQLA QIEHLQPVSS LWQPLEEPGT
PVLRRVEGEG DRVAVTYRQA GDDNILVEFG EAKLDLELRF RAHALMQWIR MRNVEGIIDL
TPGIRSLQIH FDNLRLPREK LLALLQQAEV EQTDIENLEL PSRIVHLPLS WDDEQTRLAI
EKYMQSVRKD APWCPSNIEF IRRINGLDSI DEVKRIVFDA SYLVLGLGDV YLGAPVATPL
DPRHRLVTTK YNPARTWTPE NAVGIGGSYM CVYGMEGPGG YQFVGRTTQV WNTYRQTDAF
IEQKPWLLRF FDQIRFYPVT HEELMQMRED FPLGLCQLKI EPTSFSLKQY KAFLQENDAG
IRSFKQRQQQ AFDEERARWE ASGQSNYASV TAEEEKPAEQ LSLQSGEEAA ASPVHGNIWK
VVVEEGQEVE EGDTLIIVES MKMEVPVPAP CSGTVSRVLV NSGLVAAGQS LIVIAGEAS
//