ID A0A0V1ASH7_TRISP Unreviewed; 3827 AA.
AC A0A0V1ASH7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Angiotensin-converting enzyme {ECO:0000256|RuleBase:RU361144};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361144};
GN Name=ACE {ECO:0000313|EMBL:KRY27761.1};
GN ORFNames=T01_14869 {ECO:0000313|EMBL:KRY27761.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY27761.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY27761.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY27761.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoyl-CoA + hydrogencarbonate = (2S)-ethylmalonyl-CoA
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:59520, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- SIMILARITY: Belongs to the peptidase M2 family.
CC {ECO:0000256|ARBA:ARBA00008139, ECO:0000256|RuleBase:RU361144}.
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:KRY27761.1}.
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DR EMBL; JYDH01000236; KRY27761.1; -; Genomic_DNA.
DR STRING; 6334.A0A0V1ASH7; -.
DR InParanoid; A0A0V1ASH7; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd06461; M2_ACE; 5.
DR Gene3D; 1.10.1370.30; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.30; -; 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; 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; IPR041265; PCC_BT.
DR InterPro; IPR001548; Peptidase_M2.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 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; PF18140; PCC_BT; 1.
DR Pfam; PF01401; Peptidase_M2; 5.
DR PRINTS; PR00791; PEPDIPTASEA.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 5.
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; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Carboxypeptidase {ECO:0000256|RuleBase:RU361144};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU361144}; Hydrolase {ECO:0000256|RuleBase:RU361144};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|RuleBase:RU361144};
KW Metalloprotease {ECO:0000256|RuleBase:RU361144};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Protease {ECO:0000256|RuleBase:RU361144};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|RuleBase:RU361144}.
FT DOMAIN 39..486
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..355
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 3827 AA; 439922 MW; 27CF140320A6FD9D CRC64;
MAMILFKSRP YGCNYILRRC FASDRSMYVL DPINPEEKKF QKILIANRGE IACRIIKTCK
AMGIKTVAVH SDVDSLALHV QMADEAVCIG PAPTRDSYLR MDKILQAVKD TGAEAVHPGY
GFLSENTEFA RLLTEAGGVF IGPNSKAILA MGDKIQSKRI ATEAKVSMIP GFDGEIKDAE
MCVKVANEIG YPVMIKASAG GGGKGMRIAW NDKEAREGFR LSQQEAASSF GDDRMLVEKY
IDNPRHIEMQ VLCDKHGNAI WLNERECSIQ RRNQKVIEES PSPFVPPEMR KKMGDEACAL
ALAVGYDSAG TVEFLVDSKR NFYFLEMNTR LQVEHPITEA VTGVDIVQQM IRIAYGHKLN
LKQSDIPIRG WALECRVYAE DPYKSFGLPS VGRLTRYEEP LRLNGIRCDS GIYEGSEISI
YYDPLICKLI AYANDRIETI NLMRDALDEY VIRGVTNNIP LLRDIMSEER YRSGNITTKY
LFETYPEGFH GVRLNDEETR SIAAVAAALF THHRHRAVNF LNSVQQDFSK NTQSMNEQML
FVKVPHIDRE ASQHKISGVE IIRDSCTVTL DGKKVHIEGP INFCNTVLNL KVNGKPCNVQ
IKSCDTAGRI SLLYKGCPYD LNVTTSTAEK YYKYMPAPKK VDLSNVIVAP MPGMIKSVSV
KVGQAVSECQ ETCVIEAMKM QNSLLAPKSG KAPLEQRASL EEVEEWLAKY DRDAGQLQDL
YTVQLFQYRL ELSKGLLEEF RSTGVKVIKH QLDARSGALK FLANLPKNVS VETVRQLRLI
SAQAAVDFGI WDVVLDKSKK RFVELPELML SGYSRSFACE NQTTVACCQH PIVLYPNLIA
LFSNNRTYDT LFPLWYSWGS SVQSILENQF VEFVNLANQG ARSVDYENYY NYMESSYERP
LLQTDLLQLY QSTLPIFEHL HAYVRRKLIA HYGTSRLPAS VIEAHLLGDL WAERWDALFD
LTVPYKFMPT TDVTSSLRAL NYTVESLFRL ADSWLQSAGF VKAPDSLWRL STFERFDTNA
SQTCIPTAWQ FHENDMHRVT TCAGEVSTRQ LLEAFRLLGR VQYFIQYRDR PLTFRRQAGP
GFMEAIGDTL ALFALNPASL ERLGLLFDNS TRFDVNHHHV QLNYLLRVAL TMLPSIPYHF
ALNHWQKAMF DGTISAKTMN IHWSIYRYQY SGIGRPMPSA TLDVHGTNHW SVFAVQPAYA
NLIGTVLSFQ LFQGICRAAN HTGPLHRCNL DSNPLLGRQL SNLMRLGATK PWQEALKLVS
KKALLSAEGM LEFFEPLHDW LKRENEKAHE CYGWNYKHET APIGTQLQKP RCGDFLPTNQ
NFKAEQFYNN YEAKQLALER EVRSRWWDYA TNITDHNLIR MTESMANKVA FVGEAARRAR
AEIYLPMVDD DRLARMIRLV RSRTLQLNAV DTAELNRLIG GMTSTFSRGR ICSWRPFRST
PDCKRMWSLN PDLTNLFANC HDYKTLLYAW QAWHDVVGRP IRGPFERAVQ LGNRGARAIG
YDDVGDYWRA QYENDYLKEE LASMWQQLLP LYEQLHAYVR RRLRYLYPGQ FNCTAIPAHL
FGNIWAESWV NLFPLVSPYS KAPQVDVSEE MRRQRFTPER MFRLAESFFS SVGLPNMTRT
FWQKSYLERP DDGRNFICHA SAWDMFYPDD FRIKMCTQVT MADLIVAHHE MGHVHYFMQY
ADQPSVFRSG ANPGFHEAIG DTIALSVATP SHLRLVGLYN GPVDDAHLDV NFLLKQALEK
VAFLPFGYLV DLWRWNVFRG VYSADHWNRD WWQLRHDIQG ILPAVERPRY SFDPGAKFHV
ASSTPYIRYF IAHVLQFQLY KALCQFAGHS RNHGEPLHRC DFYNSTVAGE KLALMLQLGS
SRHWRQALQL VTGERKLSVE PLKEYFQPLM DWLREENKNE CFGWGRQWPE QVQSTLMKPR
CGAFQPPDQV ELELIKLKKF LENFQILTSS LQREIDRAHW KRWTDAGNGT LLMRLLNSTT
EKALVLRNQA RQLATMNYSL LFEPTDLEMV DVILHPDTPN NDDDIRLMNE LLLKMASIGD
GAFIRKCQRV PASGVPNGTD DQRWYLIPDL MNLVSRSSVD VETLTYVWKQ WRDTVGKRMF
PLYEKYVSLT RKVELEKRTA KTDHHHHHHQ MDQLEQLTSE LLPLYEHLHT YVRRKLMVNY
RDNFTTSSIP AHLLGSMFAE DWSNLLWNVN FTTARWILEV DQSLRRKNFT VIGMFKQAEM
LFRNVGLDNL TEQFWQKSIF EQKKKNPSFE KRLLCRPALW RFPNDDQYRI GLCATVDVQQ
FLAAHSTLAR VHHLIMLSEQ QPVLSIWTGN SNVADVVSLL VRLLAENFNY LKSTDMIPTK
WNYTIDDELQ LLLFQALRIV PSLPYYLAIS RWRAQLADNG TAVWQRSWWD VRNKYQGISV
PVERQATDFD PGANVDVFLA RSTVDSFLAT VAHFQVFKSL CDRQNHKGPL HRCNLLLDHG
QHVGQTLQNV LVVPSGRNLS TLLNSLTGNS AISTSGLLEY FRPLFEWLKT ENTDDCFGWG
YQWPADINDS LPQPRCDRVL PVDPVDVETA KVSRFLNSFE KHARLVNGRL AWARWIYRTN
STDLESRIVA LEQVELEHDK FYEQQANATG KFKFDLIQNP LIIRQLYAIK DRGMYYRAEN
GLRILLNSMR KIYDTMYFFP LERQTPVDSG SLQLASVDDD RRQLASCCND YTEMYAIWEN
WHGKIGAKMK PLFEQYVQLA NMASNKAGYV DMGYWWQSRF ERYNFVQHLQ QLWYRVLPLY
ERIHARVRRL FIRRFPNKFS NSSIPAHLFG SYLFDQNCAD HFDHHSLPYP ELLSLNATEE
MISRNYTAHH LFKMAESFYE SLGFAEMNDA FWNISVFHYE TTTNSTPKDC RPLAVDFSNG
LQYAIYMCTD VSVDGLVEAH RQMARLHHYM TCAEQPSIFR HDTGIGFFRA ISDAVALSIG
TPTHLSRIGL LNISEGDVSK NMTDMNYLYK AIVRDIVSLP AGYVIDLYMW NVFNGKISSE
ELDEAWWRLR NAHQGIMPPA GHRYSGLDAA AEWRISNHGP MVGNFVATIL KFQLYKAFCE
AAGHRGPLHR CDLSNSKAVG RLLKALMKPA NSSPWYETLE QLFNISQLSV EPLFEYYQPI
VSWLEQEEGG KNDECFGWGE QWPPAVEKTL PIPRCGITMD DDTTDGAEQE LIRAENYLAS
YEQRAQTVYE DYARKRWLFL TDMVDHNRNL YVEAEVVKRL FDAEQASLVL DGNFNFSSLA
SVNQQVVSVL ERIVQSRIVK IEETQAKALA SVSAQLRTLH STTFICAVGT ANMASCPHED
RLYLEPDLVE LMAKSTDPSV LQYLWQRWHQ AIDSAAIGPS LHRHTAISNA IVRRNNFPDL
GAYWRSLYRD ANFERTVESL WIQILPLYEQ MHAYVRRMLH ARYPDSFNTS AVPVHLFGDM
FASNWLPLYA NSIPYPNVST ASAWFDERLT QNFTAEYLLK MAEKFFLNIG LLPLTEQFWN
NSIVNPNRDK RSNMECHAGT ADFFNRIDYA LKSCTGGRYL ARDFLNAFEQ VGQVEFSMIC
ADQRLKFRED DESGLREAII NMVVLTATTP LQLRDMGLIV EGPFERGSSL EAEEGVNFLY
FTALQKLASL AFAYAADLYR WRLFNGSIPQ ADYNDHWWLL KYQYQGLVAP TGLLENLTSY
HAASEHHIAN NEPLLRLFVA NVLQFQLQKS LCLESGHRGP LYQCNPLAGG SAGRRLKRML
RTVCSTGSFA DALRTIATNI SHLSAEPLLE YFQPLQRWLE TQNALAMDCY GWNHNWTTIN
VTGLVKYPRC GFYYYYNGSS AAPDAPNVKV FIVLVLLWLT RIGFDFQ
//
