Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q2NWV8

Entry ID Method Resolution Chain Position Source
AF-Q2NWV8-F1 Predicted AlphaFoldDB

No variants for Q2NWV8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2NWV8

No associated diseases with Q2NWV8

2 regional properties for Q2NWV8

Type Name Position InterPro Accession
domain Cobalamin-independent methionine synthase MetE, C-terminal/archaeal 429 - 751 IPR002629
domain Cobalamin-independent methionine synthase MetE, N-terminal 5 - 312 IPR013215

Functions

Description
EC Number 2.1.1.14 Methyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
methionine biosynthetic process The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
methylation The process in which a methyl group is covalently attached to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAILSHTLGF PRVGLHRELK KAQESYWAGN ISQQQLLETG RELRARHWQQ QKDAGVDLLP
70 80 90 100 110 120
VGDFAWYDHV LTTSLMLDNV PARHRSGANE SDIDTLFRIG RGRAPTGEPA AAAEMTKWFN
130 140 150 160 170 180
TNYHYMVPEF TLGQQFRLGW TQLLDEVDEA LALGHRVKPV LLGPVSYLWL GKVKGEAFDR
190 200 210 220 230 240
LSLLPALLPV YKQVLGELAK RGVDWVQIDE QALVLELPQA WREAYREAYQ ALQGQTKLLL
250 260 270 280 290 300
TTYFDSIRHQ LDIITALPVQ GLHVDLVAGD DDLTELHRQL PAEWVLSAGV INGRNVWRAD
310 320 330 340 350 360
LQSWFEQLRP LLGKRELWLG SSCSLLHSPI DLSTETQLDE EVKSWFAFAL QKCAELGLLR
370 380 390 400 410 420
AALNAPDEAN QARLGEYSAP IRARRHSSRV HNPEVKARLE KITAADSQRQ QPYAARAALQ
430 440 450 460 470 480
RARFKLPAWP TTTIGSFPQT TEIRGLRLDF KRGRLDGGHY RTGISEHIKQ AIVEQERLGL
490 500 510 520 530 540
DVLVHGEAER NDMVEYFGEH LDGFVFTQNG WVQSYGSRCV KPPIIIGDIS RPEAITIEWA
550 560 570 580 590 600
RYAQSLTAKP VKGMLTGPVT ILCWSFPRED VSRKTIARQI ALALRDEVAD LEQAGIGVIQ
610 620 630 640 650 660
IDEPALREGL PLKHSAWQDY LTWAVEAFRL NAAVAQDDTQ IHTHMCYCEF NDIMDSIAAL
670 680 690 700 710 720
DADVITIETS RSDMELLETF KEFDYPNEIG PGVYDIHSPN VPSEEWIVEL LRKAAQRIPA
730 740 750
ERLWVNPDCG LKTRAWPETR QSLANMVTAA RKLREEQP