ID D8SW33_SELML Unreviewed; 2192 AA.
AC D8SW33;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ11422.1};
GN ORFNames=SELMODRAFT_447020 {ECO:0000313|EMBL:EFJ11422.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ11422.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001455};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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; GL377647; EFJ11422.1; -; Genomic_DNA.
DR RefSeq; XP_002987586.1; XM_002987540.1.
DR STRING; 88036.D8SW33; -.
DR EnsemblPlants; EFJ11422; EFJ11422; SELMODRAFT_447020.
DR GeneID; 9629767; -.
DR Gramene; EFJ11422; EFJ11422; SELMODRAFT_447020.
DR KEGG; smo:SELMODRAFT_447020; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_000395_5_2_1; -.
DR InParanoid; D8SW33; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 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 Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR049074; ACCA_BT.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013537; AcCoA_COase_cen.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF21385; ACCA_BT; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
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; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 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 Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 23..533
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 176..370
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 660..734
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1443..1780
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1784..2084
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2192 AA; 242469 MW; D46348751E0554B8 CRC64;
MEANGHPHSQ VDDYCFSLGG ARPIHSILIA NNGMAAVKFM RSVRSWAYEA FGAERAVVLV
AMATPEDMRI NAEHIRMADQ FVEVPGGTNN NNYANVQLIT EVAERAGVAA VWPGWGHASE
NPDLPSSLAA RNIVFLGPPA APMAALGDKI GSSLIAQAAG VPTLPWSGSN VAVPFESCRD
GIPEELYKQA CVFSAEEALA MCQKIGYPAM IKASWGGGGK GIRKVHNDEE VKALFKQVQG
EVPGSPIFIM KVASQCRHLE VQLLCDQYGN VAALHSRDCS VQRRHQKIIE EGPITIAPPE
TVRLLEQGAR RLAQCVSYVG AATVEYLYSM ETGEFHFLEL NPRLQVEHPV TEWIAEVNLP
AAQLAVGMGI PLWKIPEIRR FYGKEDQLVH NQTNWHAAAA DTAVAFDFDT AVANKPRGHV
VAVRVTSEDP DDGFKPTTGK VQEVSFRSKP NIWAYFSVKS GGGIHEFSDS QFGHVFAFGE
TRPAAIANMV LGLKELHIRG EIHTNVDYTV DLLHAPEYKN NKIHTGWLDG RIAMRLRAER
PLWYLSVVCG AIYRTSRLCA ARVSEYIGYL EKGQIPPKNI SLVNFRTSLN IDGSKYTMEL
TKGGPGTYRL NMNNSRVEAE VHTLRDGGLL VQLDGNSHVV YGEEEAAGTR LLIDGRTCLL
QNDHDPSRLI AETPCKLMRF LVADGSHVDT DTPYAEVEVM KMCMPLLSPA SGTIHFKHLE
AQAMVAGDLI AVLDLDDPSA VRKAVPFSEG FPALGTPIPV PGKVHHRCAL IINASNMILA
GYEHNVDEVV QTLLSCLDDP QLPVLQWQEC IAVLASRIPT NLKARLDLKL KEYEASSGSE
RGAADFPAKG VREVLEEFLA SATDQDRATQ ERLVEPLLTL AKSYEGGRRG HACSIVKALF
EEYLLVEEHF SQGTGTQADV IESLRHVHKK DLWKVVDIVL SHQGIKTKNA LMLRLIEALV
YPNPSAYRDQ LVRLAALSDS NYTELAVKSS LLLEQSKLSG IRADIARSLS ELGMFTEDEN
GSKRSGKSAI DERMEYWVDA PVAVEDALVA LFDHGDHGDH TLQRRVIETY IRRLYQPYLV
KGSVRMQWQR SAMLASWQFY EEGPLRVATA AEESEPVKWR GAMAVLSSLN TLSSTVRTAL
EEWFGVTQET KDSNHTRLGN VLHIALVGRK NQMSAHQDSG DEGQTQERVE KLAKGLKGET
LRGLLQAAGV GVVSCIIQRD EGRGPIRHCF HWSQETKSYA EDPLYRHVEA PLSGFLELDN
LKELGTMKYS LSRDRQWHLY SVQEKKGKST VKRTFLRTFV RQTKTLDEDG TFESVIKALQ
GALEELEVAE GRAEHVHMYL CVLRPQGVRS LASSIVVWLE ALVHKIYAAL GTRMYRLAVL
AWELRMSLGG EGIWRVVVSN ATGYTCKVEI YREVRDPLTK QTVYSSPFPG CEGPLHGVPL
SKQCKPLEAL DSRRLLARKN GTTFCYDFPL VFEAALKQCW KESGMELPKD TTAFCATELV
FPTANQSWDA TLVETNRPSA SNDIGMVAWR LELCTPEYPQ GRHLIVVSND VTHAAGSFGP
KEDAFFKCVT DMACREKLPL VYLAANSGAR IDVAEEVRRS FQVGWLDDSR PEHGFHYLYL
RPDDYAKLGA FVNSHKLEVA DGQVRWVIDD IIGQKDGLGV ENLSGSGAIA SAYSKAYRET
FTLTYVSGKT VGIGAYLARL GMRCIQRLDQ PIILTGYSAL NKLLGREVYS SQMQLGGPKV
MATNGVTHLT VSDDLEGVSA ILNWLSYVPS VKGGGLPSRP SDDPPDRTVA YVPENSCDPR
AAVAGVYNSE GGGGWMGGIF DKGSFTETLE GWARTVVTGR ARLGGIPVGI IAVETQTVMQ
VIPADPGQLD SQERVVPQAG QVWFPDSASK TAQAMIDFNN EGLPLFILAN WRGFSGGQRD
LFEGVLQAGS TIVEHLRTYQ QPVFVYVPRN GELRGGAWVV VDSKINPDQV EMYADSTARA
GVLEAEGVAE IKFRREQILD SMKRLDPVLP RLEDPAAVRA RQDSLIPVYK QIALRFIDMH
DTAFRLAAKG IIRRVVDWEC SRSFFYNRLA RRLAQESVIQ RVLAAAGSEC SHRDALELLR
QWFLTWSSSS TGDGDGWADD TLVVEWLASN ESRIQRELQQ LRVQKVSRQM LSDCQNRNDD
LEVLPQVIRN LVDKMDPAAR QALKEQIKAA LL
//
