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 Q66FT7

Entry ID Method Resolution Chain Position Source
AF-Q66FT7-F1 Predicted AlphaFoldDB

No variants for Q66FT7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q66FT7

No associated diseases with Q66FT7

2 regional properties for Q66FT7

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 - 313 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
MTILNHTLGF PRVGLKRELK KAQESYWAGN STQEELLNVG RELRARHWQQ QQQAGVDLVP
70 80 90 100 110 120
VGDFAWYDHV LTTSLLLGNV PERHQNADGS IDIDTLFRIG RGRAPTGKPA AAAEMTKWFN
130 140 150 160 170 180
TNYHYMVPEF QQGQQFKLGW TQLLDEVDEA LALGHKIKPV LLGPITYLWL GKVKGEQFDR
190 200 210 220 230 240
LSLLNDILPV YQQVLAELAK RGIEWVQIDE PALVLELPQE WLDAYQPAYQ ALQGQVKLLL
250 260 270 280 290 300
TTYFDSIGHN IDTIRALPVQ GLHVDVVAGH DDLAVLNKNL PKEWLLSLGV INGRNVWRAD
310 320 330 340 350 360
LSSWFERLQP LVNSRPLWLG SSCSLLHSPI DLNEETRLDA EVKSWFAFAL QKCAELALLT
370 380 390 400 410 420
QALNAPNDAK LAELAAYSAP IRARRSSSRV HNAQVEQRLA AITSQDIERQ LPYEARAETQ
430 440 450 460 470 480
RKRFNLPAWP TTTIGSFPQT TEIRGLRLDF KQGRLDGKNY RTGISEHIKQ AIAEQERLGL
490 500 510 520 530 540
DVLVHGEAER NDMVEYFGEH LDGFVFTQNG WVQSYGSRCV KPPVIIGDIS RPEAITVEWA
550 560 570 580 590 600
KYAQSLTEKP VKGMLTGPVT ILCWSFPRED VSRETIAKQI ALALRDEVED LEKAGIGIIQ
610 620 630 640 650 660
IDEPALREGL PLRRADWQAY LQWAVDAFKL NAAVAQNDTQ IHTHMCYCEF NDIMDSIAAL
670 680 690 700 710 720
DADVITIETS RSDMELLESF EDFAYPNEIG PGVYDIHSPN VPSVEWIEAL LRKAAQRIPA
730 740 750
ERLWVNPDCG LKTRGWPETR QALANMVLAA QRLREEQI