ID A0A151MBU5_ALLMI Unreviewed; 1378 AA.
AC A0A151MBU5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase {ECO:0000256|ARBA:ARBA00017309};
DE EC=6.3.5.1 {ECO:0000256|ARBA:ARBA00012743};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00030681};
DE AltName: Full=NAD(+) synthetase {ECO:0000256|ARBA:ARBA00031075};
GN Name=TPCN2 {ECO:0000313|EMBL:KYO21890.1};
GN ORFNames=Y1Q_0000560 {ECO:0000313|EMBL:KYO21890.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO21890.1};
RN [1] {ECO:0000313|EMBL:KYO21890.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO21890.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005188}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000256|ARBA:ARBA00007145}.
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:KYO21890.1}.
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DR EMBL; AKHW03006283; KYO21890.1; -; Genomic_DNA.
DR eggNOG; KOG2301; Eukaryota.
DR UniPathway; UPA00253; UER00334.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005765; C:lysosomal membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0022832; F:voltage-gated channel activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07570; GAT_Gln-NAD-synth; 1.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 1.10.287.70; -; 2.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR HAMAP; MF_02090; NadE_glutamine_dep; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR028798; TPC2.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR NCBIfam; TIGR00552; nadE; 1.
DR PANTHER; PTHR46768; TWO PORE CALCIUM CHANNEL PROTEIN 2; 1.
DR PANTHER; PTHR46768:SF1; TWO PORE CHANNEL PROTEIN 2; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 710..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..775
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 918..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1060..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1134..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1173..1196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1301..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..245
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 1378 AA; 156981 MW; F90B1EFCA639B5E7 CRC64;
MARAVTVATC ALNQWALDFD GNLERILRSI EIAKHKGARY RLGPELEICG YGCSDHYYES
DTLLHSFQVL AKLLESPAAQ DIICDVGMPV MHRNIRYSCR VIFLNKHVEE YFLPRMIQEV
TGQETVPFGD AVLATKDTCL GTEICEELWA PNSPHIEMGL DGVEIFTNSS GSHHVLQKAY
IRVDLVNSAT AKNGGIYILA NQKGCDGDRL YYDGCAMISV NGDTVAQGSQ FSLDDVEVLV
ATLDLEDVRT YRAEISSRNL LASRVNSYPR VKVNFALSCS DEICVSISEP IQWRYHSPEE
EICLGPACWL WDYLRRSKQA GFLLPLSGGT DSSATACIVY SMCHQVCLAV KNGNQGVLTD
VRRIVNEDTY TPEVPQEFCR RIFTTCYMAS ENSSQDTRNR AKFLAEQIGS YHINLNIDVA
VKAIVGIFSI VMGKSPQFRV YGGSSRENLA LQNVQARLRM VLAYLFAQLS LWARGMPGGL
LVLGSANVDE SLRGYLTKYD CSSADLNPIG GISKTDLKSF LQYCIENFQL TSLRSILSAL
PTAELEPLAD GQVSQIDEMD MGMTYAELSI YGKLRKVAKA GPYSMFCKLI NMWKEICSPR
EVASKVKHFF RMYSVNRHKM TTLTPAYHAE NYSPDDNRFD LRPFLYNSAW SWQFRCIDKQ
VSKLETAGAD CDLYINQAVV FIEDAIQYRS INHRVDSKSL WLYRWYYSRI CQWILGLTIT
IILGLAFIET PSSLTVTSDI RYRSPAWEPP CGLTESIELL CFLIFIADVS VKSYLIGWEE
FRKTKWLMAY ILALVVSLTD WTVSMSFSCR ETVRIRRILR PFFLLQNSSM MKKTLKSINS
TLPEMASVVL LLAVHLSLFT MFGMLLFART KDGQQDKEWL GYFRNLPDAL TSLLVLLTTA
NNPDVMIPAY SKNRAYSIFF VLFTVLGNLF LMNLLTAIIY NQFRGYLLKS VQSSLLRRRL
GIRAAFEVLC SLKETPAHTH ELCVNAETLL RVLKKVDMDF GCKHVILRTL RTCPHGLLSA
VQFQKLFEEL DKDSVKQHPA KPEYQSPFLQ KMQFAFGHPY FSYTGNVVAL ANIISICVVL
VIDADKQPSE RDDFFLGAIN FFFILYYLLE MLLKIMAMGL RRYLSYPSNR FDGLLTGILL
VLEISTFAVY GFPHPGWRPE MMGLLSLWDM VRLVNMLIVF RFLRIIPNMK FMALVISTLL
DLVKNLRAFA GILLVVYYAF ALIGIALFKG AIVPMGNISV VNITSGNNTL QCGTYEQLEY
WPNNFDDFAA ALVTLWDVMV VNNWQVFLDA FSRYSSPWSK LYFVAWWLIS SVIWVNLFVA
LLLENFIHKW DRRCQQQSLS EIEYQVTMEL MFRDVLEEPT EEELMEKLYQ HPHLQLCR
//
