ID D3SS70_NATMM Unreviewed; 682 AA.
AC D3SS70;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein {ECO:0000313|EMBL:ELY24962.1};
DE SubName: Full=Molybdopterin molybdenumtransferase {ECO:0000313|EMBL:ADD04796.1};
DE EC=2.10.1.1 {ECO:0000313|EMBL:ADD04796.1};
GN Name=moeA2 {ECO:0000313|EMBL:ADD04796.1};
GN OrderedLocusNames=Nmag_1214 {ECO:0000313|EMBL:ADD04796.1};
GN ORFNames=C500_18588 {ECO:0000313|EMBL:ELY24962.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD04796.1, ECO:0000313|Proteomes:UP000001879};
RN [1] {ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000001879};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA Maupin-Furlow J.A., Woyke T.;
RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD04796.1, ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD04796.1}, and ATCC 43099 / DSM
RC 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT "A comparative genomics perspective on the genetic content of the
RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL BMC Genomics 13:165-165(2012).
RN [3] {ECO:0000313|EMBL:ELY24962.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC {ECO:0000313|EMBL:ELY24962.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:ADD04796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD04796.1};
RA Pfeiffer F.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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DR EMBL; CP001932; ADD04796.1; -; Genomic_DNA.
DR EMBL; AOHS01000057; ELY24962.1; -; Genomic_DNA.
DR RefSeq; WP_004217104.1; NZ_AOHS01000057.1.
DR AlphaFoldDB; D3SS70; -.
DR STRING; 547559.Nmag_1214; -.
DR PaxDb; 547559-Nmag_1214; -.
DR GeneID; 8824046; -.
DR KEGG; nmg:Nmag_1214; -.
DR PATRIC; fig|547559.17.peg.3666; -.
DR eggNOG; arCOG00217; Archaea.
DR HOGENOM; CLU_010186_3_0_2; -.
DR OrthoDB; 31371at2157; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001879; Chromosome.
DR Proteomes; UP000011543; Unassembled WGS sequence.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00887; MoeA; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR InterPro; IPR024370; PBP_domain.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF12727; PBP_like; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 4: Predicted;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000001879};
KW Transferase {ECO:0000313|EMBL:ADD04796.1}.
FT DOMAIN 206..347
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 124..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 71478 MW; 76016C88BBB7AE54 CRC64;
MNRKEFRDLA SPTEAREAID SLSIEGGVER VSLEDARGRV LVARLDAELD VPGFDRASLD
GYALNARDTF GADEADPAEL DVVGTVHAGE EPGVVLESGQ AAEISTGAVM PDGADAMVPV
ERTDVGGDVD DRTDENGESG EDHESNETVL VRTSVAPGDN VMFAGADVAA GERALGPGTR
ITPRDIGLLS ALGIDEVPVR RKPRVGIVST GDELVRPGGD GELESTRGEI YDVNSYTIAA
GVEDAGGEAV LYPHAGDEQD EMERILREAA AECDLVLSSG STSASAVDVI YRVIEEQGEL
LLHGVSVKPG KPMLVGRLDS SAYVGLPGYP VSAMMVFRTF VAPAIRRAAG LPEPESATVT
GRMARDERYG EGRLRLMPVG LVTDGDGGGG GNGNGAGATA GNGAGASDTL VYPVDKGSGA
TTSLAEADGV VEVGPETDYL ERGESVDVQL FSPDVRPPTL LGVGEDDPTL NRVLDRLDNP
RYLSVGSRPG LRRLREGIPD VAVVAGPSGR EHGLEATELG SWERDWGLVV RAGNPDEIDG
LDDLVDRDLQ FVNRTSDSGL RTSLERALAD LAAERDAETG TGTGTGTETG TKTDHHNLAT
QIDGFDVGLR AHESPARRVI AGEADAALGL RDTAERLSLE YVPLGTQTMH VLANPDRVEK
ASVRELESVL ADAVVDDEGL SL
//
