ID G3XMY7_ASPNA Unreviewed; 1075 AA.
AC G3XMY7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=phosphatidylserine decarboxylase {ECO:0000256|ARBA:ARBA00012243};
DE EC=4.1.1.65 {ECO:0000256|ARBA:ARBA00012243};
DE Flags: Fragment;
GN ORFNames=ASPNIDRAFT_202968 {ECO:0000313|EMBL:EHA28450.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA28450.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA28450.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|ARBA:ARBA00001928};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis. {ECO:0000256|ARBA:ARBA00024326}.
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:EHA28450.1}.
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; ACJE01000001; EHA28450.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XMY7; -.
DR SMR; G3XMY7; -.
DR STRING; 380704.G3XMY7; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1080105; -.
DR HOGENOM; CLU_002661_0_0_1; -.
DR UniPathway; UPA00558; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04039; C2_PSD; 1.
DR CDD; cd04024; C2A_Synaptotagmin-like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD-B.
DR InterPro; IPR033179; PSD_type2_pro.
DR NCBIfam; TIGR00163; PS_decarb; 1.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 22..139
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 239..363
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 502..537
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1075
FT /evidence="ECO:0000313|EMBL:EHA28450.1"
SQ SEQUENCE 1075 AA; 120038 MW; 5B655383A8D82383 CRC64;
MVRLPLPQRL SSHLSTKSNN PTPGQSRSTS PMRMPEQKPL ILKVSVIRGR DLAAKDRGGT
SDPYLVVTLG DARQSTPTIP KTLNPEWNVT FEMPVVGVPL LECICWDHDR FGKDYLGEFD
IPLEDIFQNG DVHQQPKWYT LKSKRKPTKK KDSMVSGEIL LQFSLLDSSN PTASPTDTYH
KFRTLVSSGD EEDDFPQIPS ITLDDADREE ETSDETDDPT KPEVVEKRRR RLRLKRLKRK
SLAARAYQFS GAGNGVQGIV FMEIVKVTDL PPERNVTRTS FDMDPFVVTS LGRKTLRTPV
VRHNLNPIYN EKMVFQVMKH EQSYTIGFTV MDRDKFSGND FVASASFPVQ TLIKSAPEAD
PETGLYKFVD PTLDPAGAEQ GHSSRPSEIR IAISRSPSAN SLSTSPKFGT TPRGSSTSLS
SQTLLEQSST LLPPRSIPEV PESSQPSTPT TAGFEGDPIG PLESNGLQVY RIQLALKNKE
RWEDKHFPEL FVKAKYMPYR ALRQQFWRLM LRQYDADESG RIDKVELTTM LDTLGSTLKE
STIDSFFERF SLENQPSETM DLTFDQAVIC LEDTLQALQK DPSSPPKKLS PTPSTASRES
DEQSSGDELT MEPGSHNANP QTTSVPTLPT DEQPSSTEED LLPDDLGDER GVEHVIELRE
CPLCHQPRLS SRSDADIITH IATCASRDWR QVDNLVMGGF VTSSQAQRKW YTKVITKISY
GGYKLGANSA NILVQDRITG QINEERMSVY VRLGIRLLYK GLKSREMEKK RIRKILKSLS
IKQGRKYDDP ASASQIRDFI NFHQLDMSEV LLPVEKFKTF NEFFYRALKP GARPCSAPDE
PGIVVSPADC RAVVFDRMEE ATGIWVKGRE FSVARLLGDA YPEDVQRFKN GALGIFRLAP
QDYHRFHIPV DGVLGEPKTI EGEYYTVNPM AIRSALDVYG ENVRVLVPID SVAHGRVMVV
CVGAMMVGST VITRQAGEKV SRAEELGYFK FGGSTLLLLF EEGAVNFDSD LVDNSKGPLE
TLIRVGMSVG HSPGVAQFEP DMPKKSEDVS LEEMQAAKRR IEGSLAPPTD AAAFE
//
